satarupa22/MacromolecularLigandDB huggingface dataset:
Crystal structure of human CaMKII-alpha (CAMK2A)kinase domain (PDB entry 6VZK)
Macromolecule: Calcium/calmodulin-dependent protein kinase type II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.17
Sequence length: 268 residues
Sequence: TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHR
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.55
R work: 0.2103
R free: 0.2944
Average B factor: 34.924
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7
Crystallization temperature (K): 277
Crystal growth procedure: PEG 6000, 50 mM HEPES, 3-Aminobenzene-sulfonic acid, 5-Sulfosalicylic acid dihydrate,  p-Coumaric acid, PIPES, Terephthalic acid, Vanillic acid
Matthews coefficient: 2.19
Solvent content (%): 43.77
Ligand: 4'-HYDROXYCINNAMIC ACID (HC4)
Ligand formula: C9 H8 O3
Ligand molecular weight: 164.158
Ligand SMILES: c1cc(ccc1C=CC(=O)O)O
Ligand InChI: InChI=1S/C9H8O3/c10-8-4-1-7(2-5-8)3-6-9(11)12/h1-6,10H,(H,11,12)/b6-3+
Release date: 2020-04-22
Thrombin in complex with D-Phe-Pro-2-chlorofuran derivative (13l) (PDB entry 6ZGO)
Macromolecule: Prothrombin
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.21.5
Sequence length: 36 residues
Sequence: TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
Oligomeric state: Hetero 3-mer
Stoichiometry: A1, B1, C1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.79
R work: 0.1852
R free: 0.225
Average B factor: 34.9541
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 277
Crystal growth procedure: 20mM sodium dihydrogen phosphate ph 7.5
350mM NaCl
27% PEG 8000
Matthews coefficient: 2.83
Solvent content (%): 56.54
Ligand: SODIUM ION ()
Ligand formula: Na
Ligand molecular weight: 22.99
Ligand SMILES: [Na+]
Ligand InChI: InChI=1S/Na/q+1
Release date: 2021-06-30
HUMAN IDO1 IN COMPLEX WITH COMPOUND 4 (PDB entry 6WPE)
Macromolecule: Indoleamine 2,3-dioxygenase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 1.13.11.52
Sequence length: 394 residues
Sequence: MISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.43
R work: 0.1979
R free: 0.235
Crystallization method: VAPOR DIFFUSION
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 mM Tris pH 8.0, 20% (w/v) PEG6000, 0.2 M NaCl
Matthews coefficient: 3
Solvent content (%): 59.06
Ligand: 4-chloro-N-{[1-(3-chlorobenzene-1-carbonyl)-1,2,3,4-tetrahydroquinolin-6-yl]methyl}benzamide (U6G)
Ligand formula: C24 H20 Cl2 N2 O2
Ligand molecular weight: 439.334
Ligand SMILES: c1cc(cc(c1)Cl)C(=O)N2CCCc3c2ccc(c3)CNC(=O)c4ccc(cc4)Cl
Ligand InChI: InChI=1S/C24H20Cl2N2O2/c25-20-9-7-17(8-10-20)23(29)27-15-16-6-11-22-18(13-16)4-2-12-28(22)24(30)19-3-1-5-21(26)14-19/h1,3,5-11,13-14H,2,4,12,15H2,(H,27,29)
Release date: 2021-03-10
Crystal structure of Lysosomal Phospholipase A2 crystallized in the presence of methyl arachidonyl fluorophosphonate (tetragonal form) (PDB entry 4X93)
Macromolecule: Group XV phospholipase A2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1
Sequence length: 380 residues
Sequence: GAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.6
R work: 0.1986
R free: 0.2182
Average B factor: 62.707
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 277
Crystal growth procedure: 100 mM HEPES pH 7.5, 30% PEG MME 550, 50 mM MgCl2
Matthews coefficient: 4.01
Solvent content (%): 69.36
Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose (NAG)
Ligand formula: C8 H15 N O6
Ligand molecular weight: 221.208
Ligand SMILES: CC(=O)NC1C(C(C(OC1O)CO)O)O
Ligand InChI: InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
Release date: 2015-03-25
Crystal structure of MavC/UBE2N-Ub complex (PDB entry 6KG6)
Macromolecule: MavC
Type: Protein, polypeptide(L)
Source organism: Legionella pneumophila
Sequence length: 383 residues
Sequence: GPLGSEKTGLHVHEKIKHMVKNYGTMITGIPAEILGQNEAEISVGYVKKMGNMKENIAEVVRKSEMTQPTNSAGKASNEVCDLLLGTEGASEFEKSSYQVLSGDGSNLKGSLPNKNLLVRVEMDRFNAPQKYQKIKREEFNPETAEKNKIYLLEDQLVYLDIFGKVIDLGQTSDTCHRLFNAITTPFYQNYILYDEYIDPEESAEEAAMFEMGEIVKAKMKNIDCWTATHSFTIFVPESDSEDTRTLYPYQAYWTSHTLQQWFSGDKDEKLSRLGIDGYIEKLALLGTTTDSKIRSSIYGELFSPPGKEHVFCTGMNEKFSPLRVKFKVTEVNPEIALQNLEEVQEFIDTNYPGENAKDQCELYKIKAQEAMTKQLEMRLLIE
Oligomeric state: Hetero 3-mer
Stoichiometry: A1, B1, C1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.39
R work: 0.1902
R free: 0.2448
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 291
Crystal growth procedure: PEG 4000, Tris
Matthews coefficient: 2.71
Solvent content (%): 54.67
Release date: 2020-04-01
The ATAD2 bromodomain in complex with compound 4 (PDB entry 6HI3)
Macromolecule: ATPase family AAA domain-containing protein 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.6.1.3
Sequence length: 130 residues
Sequence: SMQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESR
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.4
R work: 0.2924
R free: 0.3368
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.5
Crystallization temperature (K): 277
Crystal growth procedure: 2M (NH4)2SO4, 0.1M Bis-Tris pH 5.5
Matthews coefficient: 3.91
Solvent content (%): 68.57
Ligand: 2-azanyl-~{N}-(4-ethanoyl-1,3-thiazol-2-yl)-2-methyl-propanamide (G7B)
Ligand formula: C9 H13 N3 O2 S
Ligand molecular weight: 227.283
Ligand SMILES: CC(=O)c1csc(n1)NC(=O)C(C)(C)N
Ligand InChI: InChI=1S/C9H13N3O2S/c1-5(13)6-4-15-8(11-6)12-7(14)9(2,3)10/h4H,10H2,1-3H3,(H,11,12,14)
Release date: 2019-02-20
Human Aldose Reductase in complex with ALR25 (PDB entry 6TUC)
Macromolecule: aldose reductase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 1.1.1.300
Sequence length: 316 residues
Sequence: MASRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.06
R work: 0.1264
R free: 0.1433
Average B factor: 10.6
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5
Crystallization temperature (K): 291
Crystal growth procedure: PEG 6000, DTT, diammonium hydrogen citrate, NADP+
Matthews coefficient: 2.18
Solvent content (%): 43.5
Ligand: 2-(2-((3-boronobenzyl)carbamoyl)-5-fluorophenoxy)acetic acid (NXK)
Ligand formula: C16 H15 B F N O6
Ligand molecular weight: 347.103
Ligand SMILES: B(c1cccc(c1)CNC(=O)c2ccc(cc2OCC(=O)O)F)(O)O
Ligand InChI: InChI=1S/C16H15BFNO6/c18-12-4-5-13(14(7-12)25-9-15(20)21)16(22)19-8-10-2-1-3-11(6-10)17(23)24/h1-7,23-24H,8-9H2,(H,19,22)(H,20,21)
Release date: 2021-01-27
Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta-pNP (PDB entry 5GGN)
Macromolecule: Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.1
Sequence length: 164 residues
Sequence: GPLGSGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAE
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.211
R work: 0.1439
R free: 0.1657
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8.8
Crystallization temperature (K): 293
Crystal growth procedure: Tris-HCl, PEG-6000
Matthews coefficient: 2.51
Solvent content (%): 51.09
Ligand: 4-nitrophenyl 2-acetamido-2-deoxy-beta-D-glucopyranoside (LEC)
Ligand formula: C14 H18 N2 O8
Ligand molecular weight: 342.301
Ligand SMILES: CC(=O)NC1C(C(C(OC1Oc2ccc(cc2)[N+](=O)[O-])CO)O)O
Ligand InChI: InChI=1S/C14H18N2O8/c1-7(18)15-11-13(20)12(19)10(6-17)24-14(11)23-9-4-2-8(3-5-9)16(21)22/h2-5,10-14,17,19-20H,6H2,1H3,(H,15,18)/t10-,11-,12-,13-,14-/m1/s1
Release date: 2016-08-10
Ubiquitin variant UbV.k.2 in complex with Ube2k (PDB entry 7MYH)
Macromolecule: Ubiquitin-conjugating enzyme E2 K
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.2.23
Sequence length: 201 residues
Sequence: MAANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.394
R work: 0.2063
R free: 0.2487
Average B factor: 61.592
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 289
Crystal growth procedure: 0.2 M sodium citrate tribasic trihydrate, 0.1 M Bis-Tris propane, pH 7.5, 20% PEG3350
Matthews coefficient: 3.04
Solvent content (%): 57
Ligand: GLYCEROL (GOL)
Ligand formula: C3 H8 O3
Ligand molecular weight: 92.094
Ligand SMILES: C(C(CO)O)O
Ligand InChI: InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
Release date: 2021-08-25
Structure of human UCHL1 in complex with CG341 inhibitor (PDB entry 8PW1)
Macromolecule: Ubiquitin carboxyl-terminal hydrolase isozyme L1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.19.12
Sequence length: 227 residues
Sequence: GPGSMQLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.2
R work: 0.2273
R free: 0.2712
Average B factor: 80.79
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 2.49 M ammonium sulfate, 85 mM trisodium citrate
Matthews coefficient: 2.37
Solvent content (%): 48.13
Ligand: (2~{S})-4-(iminomethyl)-1-methyl-~{N}-[1-[4-(pent-4-ynylcarbamoyl)phenyl]imidazol-4-yl]piperazine-2-carboxamide (GKO)
Ligand formula: C22 H27 N7 O2
Ligand molecular weight: 421.495
Ligand SMILES: CN1CCN(CC1C(=O)Nc2cn(cn2)c3ccc(cc3)C(=O)NCCCC#C)C=N
Ligand InChI: InChI=1S/C22H27N7O2/c1-3-4-5-10-24-21(30)17-6-8-18(9-7-17)29-14-20(25-16-29)26-22(31)19-13-28(15-23)12-11-27(19)2/h1,6-9,14-16,19,23H,4-5,10-13H2,2H3,(H,24,30)(H,26,31)
Release date: 2024-01-31
Crystal Structure of SETD2 bound to Compound 2 (PDB entry 7LZB)
Macromolecule: Histone-lysine N-methyltransferase SETD2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.1.1.359
Sequence length: 278 residues
Sequence: GETSVPPGSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.28
R work: 0.2054
R free: 0.2636
Average B factor: 72.212
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 M Potassium thiocyanate, 0.1M Tris pH 7.8, 25% w/v PEG 2000 MME
Matthews coefficient: 2.41
Solvent content (%): 48.9
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2021-09-22
crystal structure of the RARalpha/RXRalpha ligand binding domain heterodimer in complex with a fragment of SRC1 coactivator (PDB entry 7AOS)
Macromolecule: Retinoic acid receptor RXR-alpha
Type: Protein, polypeptide(L)
Source organism: Mus musculus
Sequence length: 238 residues
Sequence: SANEDMPVEKILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQAT
Oligomeric state: Hetero 4-mer
Stoichiometry: A1, B1, C1, D1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.55
R work: 0.205
R free: 0.2623
Average B factor: 75.71
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 24% PEG 3350, 0.2M Na acetate, 0.1M Bis Tris Propane pH 7.0
Matthews coefficient: 2.33
Solvent content (%): 47.23
Ligand: 6-[1-(3,5,5,8,8-PENTAMETHYL-5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)CYCLOPROPYL]PYRIDINE-3-CARBOXYLIC ACID (LG2)
Ligand formula: C24 H29 N O2
Ligand molecular weight: 363.493
Ligand SMILES: Cc1cc2c(cc1C3(CC3)c4ccc(cn4)C(=O)O)C(CCC2(C)C)(C)C
Ligand InChI: InChI=1S/C24H29NO2/c1-15-12-18-19(23(4,5)9-8-22(18,2)3)13-17(15)24(10-11-24)20-7-6-16(14-25-20)21(26)27/h6-7,12-14H,8-11H2,1-5H3,(H,26,27)
Release date: 2021-08-04
Sirtuin 2 protein with H3K18 myristoylated peptide and intact NAD molecule (PDB entry 6L66)
Macromolecule: NAD-dependent protein deacetylase sirtuin-2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1.286
Sequence length: 304 residues
Sequence: GSQKERLLDELTLEGVARYMQSQRCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQ
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.169
R work: 0.1738
R free: 0.2339
Average B factor: 41.3592
Crystallization method: EVAPORATION
Crystallization pH: 6.5
Crystallization temperature (K): 291.15
Crystal growth procedure: 0.1M MES, pH 6.5, 6%-20% (w/v) PEG 10000
Matthews coefficient: 2.32
Solvent content (%): 47.01
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2020-11-04
CRYSTAL STRUCTURE OF HUMAN TANKYRASE-2 IN COMPLEX WITH A PYRANOPYRIDONE INHIBITOR (PDB entry 5C5Q)
Macromolecule: Tankyrase-2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.2.30
Sequence length: 191 residues
Sequence: MHHHHHHSSGVDLGTENLYFQSMLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAM
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2
R work: 0.191
R free: 0.22
Average B factor: 32.2
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 298
Crystal growth procedure: 30-40% PEG 3350, 5% SATURATED AMMONIUM  SULFATE, 0.1M TRIS PH 8.5
Matthews coefficient: 2.43
Solvent content (%): 49.31
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2015-08-12
Crystal structure of SIAH1 SBD bound to Axin2 peptide (PDB entry 8HEO)
Macromolecule: E3 ubiquitin-protein ligase SIAH1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.2.27
Sequence length: 194 residues
Sequence: KVANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.53
R work: 0.207
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 277
Crystal growth procedure: 0.1M Bis-tris propane pH 8.0, 24% PEG 6000
Matthews coefficient: 2.28
Solvent content (%): 46.11
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2023-11-15
Crystal Structure of Human BACE-1 in Complex with Compound NB-360 (compound 54) (PDB entry 7B1Q)
Macromolecule: Beta-secretase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.23.46
Sequence length: 402 residues
Sequence: GPDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNI
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.94
R work: 0.189
R free: 0.218
Average B factor: 32.2
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6
Crystallization temperature (K): 292
Crystal growth procedure: 15% PEG 1,500 in water
Matthews coefficient: 2.11
Solvent content (%): 41.69
Ligand: ~{N}-[3-[(3~{R},6~{R})-5-azanyl-3,6-dimethyl-6-(trifluoromethyl)-2~{H}-1,4-oxazin-3-yl]-4-fluoranyl-phenyl]-5-cyano-3-methyl-pyridine-2-carboxamide (SLK)
Ligand formula: C21 H19 F4 N5 O2
Ligand molecular weight: 449.401
Ligand SMILES: Cc1cc(cnc1C(=O)Nc2ccc(c(c2)C3(COC(C(=N3)N)(C)C(F)(F)F)C)F)C#N
Ligand InChI: InChI=1S/C21H19F4N5O2/c1-11-6-12(8-26)9-28-16(11)17(31)29-13-4-5-15(22)14(7-13)19(2)10-32-20(3,18(27)30-19)21(23,24)25/h4-7,9H,10H2,1-3H3,(H2,27,30)(H,29,31)/t19-,20+/m0/s1
Release date: 2021-04-28
JAK3 kinase domain in complex with 1-[(3S)-1-isobutylsulfonyl-3-piperidyl]-3-(5H-pyrrolo[2,3-b]pyrazin-2-yl)urea (PDB entry 4QT1)
Macromolecule: Tyrosine-protein kinase JAK3
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 314 residues
Sequence: CQDPTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGSERDVPALSRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLWSGSRGCETHAFTAHPEGKHHSLSFS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.4
R work: 0.20696
R free: 0.27256
Average B factor: 32.143
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6
Crystallization temperature (K): 293
Crystal growth procedure: 30% PEG 3350, 0.1M MES, 0.2M MgCl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Matthews coefficient: 2.24
Solvent content (%): 45.02
Ligand: 1-{(3S)-1-[(2-methylpropyl)sulfonyl]piperidin-3-yl}-3-(5H-pyrrolo[2,3-b]pyrazin-2-yl)urea (3C9)
Ligand formula: C16 H24 N6 O3 S
Ligand molecular weight: 380.465
Ligand SMILES: CC(C)CS(=O)(=O)N1CCCC(C1)NC(=O)Nc2cnc3c(n2)cc[nH]3
Ligand InChI: InChI=1S/C16H24N6O3S/c1-11(2)10-26(24,25)22-7-3-4-12(9-22)19-16(23)21-14-8-18-15-13(20-14)5-6-17-15/h5-6,8,11-12H,3-4,7,9-10H2,1-2H3,(H,17,18)(H2,19,20,21,23)/t12-/m0/s1
Release date: 2015-05-27
SYK catalytic domain complexed with a potent and orally bioavailable benzisothiazole inhibitor (PDB entry 5CY3)
Macromolecule: Tyrosine-protein kinase SYK
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 291 residues
Sequence: MALEEIRPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVTDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYDVENRPGFAAVELRLRNYYYDVVNEGHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.76
R work: 0.1699
R free: 0.1947
Average B factor: 26.13
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.1
Crystallization temperature (K): 293
Crystal growth procedure: PEG 3350 20%, ammonium acetate 0.2M
Matthews coefficient: 2.17
Solvent content (%): 43.38
Ligand: (5R)-5-[(1R)-1-{[6-(1-methyl-1H-pyrazol-4-yl)-2,1-benzothiazol-4-yl]oxy}ethyl]-1,3-oxazolidin-2-one (55Y)
Ligand formula: C16 H16 N4 O3 S
Ligand molecular weight: 344.388
Ligand SMILES: CC(C1CNC(=O)O1)Oc2cc(cc3c2csn3)c4cnn(c4)C
Ligand InChI: InChI=1S/C16H16N4O3S/c1-9(15-6-17-16(21)23-15)22-14-4-10(11-5-18-20(2)7-11)3-13-12(14)8-24-19-13/h3-5,7-9,15H,6H2,1-2H3,(H,17,21)/t9-,15-/m1/s1
Release date: 2015-09-23
Crystal structure of RAF kinase domain bound to the inhibitor 2a (PDB entry 6CAD)
Macromolecule: Serine/threonine-protein kinase B-raf
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 284 residues
Sequence: GAMDRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHASETKFEMKKLIDIARQTARGMDYLHAKSIIHRDLKSNNIFLHEDNTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDSNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIEMVGRGSLSPDLSKVRSNCPKRMKRLMAECLKKKRDERPSFPRILAEIEELARELSG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.55
R work: 0.2547
R free: 0.277
Average B factor: 97.9672
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 293
Crystal growth procedure: 30% PEG 3350, 0.1M Bis-Tris Propane pH 6.5, 0.2M Sodium Nitrate
Matthews coefficient: 2.11
Solvent content (%): 41.72
Ligand: 1-(propan-2-yl)-3-({3-[3-(trifluoromethyl)phenyl]isoquinolin-8-yl}ethynyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine (EU4)
Ligand formula: C26 H19 F3 N6
Ligand molecular weight: 472.464
Ligand SMILES: CC(C)n1c2c(c(n1)C#Cc3cccc4c3cnc(c4)c5cccc(c5)C(F)(F)F)c(ncn2)N
Ligand InChI: InChI=1S/C26H19F3N6/c1-15(2)35-25-23(24(30)32-14-33-25)21(34-35)10-9-16-5-3-6-17-12-22(31-13-20(16)17)18-7-4-8-19(11-18)26(27,28)29/h3-8,11-15H,1-2H3,(H2,30,32,33)
Release date: 2018-02-21
Human carbonic anhydrase II containing 6-fluorotryptophanes. (PDB entry 8B29)
Macromolecule: Carbonic anhydrase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.1
Sequence length: 258 residues
Sequence: HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.7
R work: 0.1623
R free: 0.2098
Average B factor: 15.3913
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8
Crystallization temperature (K): 293
Crystal growth procedure: 2.9 M ammonium sulfate, 0.1 M Tris-HCl
Matthews coefficient: 2.08
Solvent content (%): 40.78
Ligand: ZINC ION (ZN)
Ligand formula: Zn
Ligand molecular weight: 65.409
Ligand SMILES: [Zn+2]
Ligand InChI: InChI=1S/Zn/q+2
Release date: 2023-01-18