satarupa22/MacromolecularLigandDB huggingface dataset:
Crystal structure of IRAK4 in complex with compound 12 (PDB entry 5UIS)
Macromolecule: Interleukin-1 receptor-associated kinase 4
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 323 residues
Sequence: MHHHHHHGGENLYFQGENKSLEVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.5
R work: 0.234
R free: 0.25
Average B factor: 52.38
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 295
Crystal growth procedure: 1.6-1.6M Ammonium Citrate, pH 7.0
Matthews coefficient: 2.49
Solvent content (%): 50.52
Ligand: 4-{[(3R)-piperidin-3-yl]oxy}-6-[(propan-2-yl)oxy]quinoline-7-carboxamide (8C1)
Ligand formula: C18 H23 N3 O3
Ligand molecular weight: 329.394
Ligand SMILES: CC(C)Oc1cc2c(ccnc2cc1C(=O)N)OC3CCCNC3
Ligand InChI: InChI=1S/C18H23N3O3/c1-11(2)23-17-9-13-15(8-14(17)18(19)22)21-7-5-16(13)24-12-4-3-6-20-10-12/h5,7-9,11-12,20H,3-4,6,10H2,1-2H3,(H2,19,22)/t12-/m1/s1
Release date: 2017-05-24
Structure of the Epigenetic Oncogene MMSET and inhibition by N-Alkyl Sinefungin Derivatives (PDB entry 5LT6)
Macromolecule: Histone-lysine N-methyltransferase SETD2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.1.1.43
Sequence length: 295 residues
Sequence: MHHHHHHSSGRENLYFQGETSVPPGSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.05
R work: 0.179
R free: 0.231
Average B factor: 59.623
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 0.1MHepes,pH7.3, 0.1MKSCN, 25-30%MPEG2000.
Matthews coefficient: 1.89
Solvent content (%): 34.96
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: 2016-10-05
Crystal structure of the WWP2 HECT domain in complex with H301, a Helicon Polypeptide (PDB entry 8EI5)
Macromolecule: H301
Type: Protein, polypeptide(L)
Source organism: synthetic construct
Sequence length: 19 residues
Sequence: XDPADRRCIQAARVCAVLX
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.6
R work: 0.2132
R free: 0.262
Average B factor: 39.6568
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6
Crystallization temperature (K): 291
Crystal growth procedure: 0.1M Sodium acetate, 0.1M sodium citrate pH6.0, 10% PEG4000
Matthews coefficient: 2.47
Solvent content (%): 50.17
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: 2023-10-25
Human Argonaute2-miR-122 bound to a seed and supplementary paired target (PDB entry 6N4O)
Macromolecule: RNA (5'-R(P*UP*GP*GP*AP*GP*UP*GP*UP*GP*AP*CP*AP*AP*UP*GP*GP*UP*GP*UP*UP*U)-3')
Type: RNA, polyribonucleotide
Source organism: Homo sapiens
Sequence length: 21 residues
Sequence: UGGAGUGUGACAAUGGUGUUU
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.899
R work: 0.2073
R free: 0.2573
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8
Crystallization temperature (K): 293
Crystal growth procedure: 26% MPD, 5% PEG 3350, 50 mM imidazole pH 8
Matthews coefficient: 2.47
Solvent content (%): 50.28
Release date: 2019-05-08
Pim1 in complex with 4-((6-hydroxybenzofuran-3-yl)methyl)benzoic acid and Pimtide (PDB entry 8AFR)
Macromolecule: Serine/threonine-protein kinase pim-1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 309 residues
Sequence: SMLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIGGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSPGPS
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.15
R work: 0.1642
R free: 0.1909
Average B factor: 49.77
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7
Crystallization temperature (K): 291.15
Crystal growth procedure: 100 mM bis-tris-propane (pH7.0), 10 % ethylene glycol, 0.3% DMSO, 20% PEG3350, 200 mM LiCl
Matthews coefficient: 3
Solvent content (%): 59.4
Ligand: 4-((6-hydroxybenzofuran-3-yl)methyl)benzoic acid (M0F)
Ligand formula: C16 H12 O4
Ligand molecular weight: 268.264
Ligand SMILES: c1cc(ccc1Cc2coc3c2ccc(c3)O)C(=O)O
Ligand InChI: InChI=1S/C16H12O4/c17-13-5-6-14-12(9-20-15(14)8-13)7-10-1-3-11(4-2-10)16(18)19/h1-6,8-9,17H,7H2,(H,18,19)
Release date: 2023-02-01
Structure-Based Design of ASK1 Inhibitors as Potential First-in-Class Agents for Heart Failure (PDB entry 5UOX)
Macromolecule: Mitogen-activated protein kinase kinase kinase 5
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.25
Sequence length: 271 residues
Sequence: LLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKV
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.5
R work: 0.228
R free: 0.253
Average B factor: 76.267
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6
Crystallization temperature (K): 277
Crystal growth procedure: 6% polyethylene glycol 2000 MME ,0.05M Ammonium Sulphate, 0.1M MES, pH 6.0
Matthews coefficient: 3.17
Solvent content (%): 61.16
Ligand: 2-(6-{4-[(2R)-1-hydroxypropan-2-yl]-4H-1,2,4-triazol-3-yl}pyridin-2-yl)-6-[(propan-2-yl)oxy]-2,3-dihydro-1H-isoindol-1-one (8GY)
Ligand formula: C21 H23 N5 O3
Ligand molecular weight: 393.439
Ligand SMILES: CC(C)Oc1ccc2c(c1)C(=O)N(C2)c3cccc(n3)c4nncn4C(C)CO
Ligand InChI: InChI=1S/C21H23N5O3/c1-13(2)29-16-8-7-15-10-25(21(28)17(15)9-16)19-6-4-5-18(23-19)20-24-22-12-26(20)14(3)11-27/h4-9,12-14,27H,10-11H2,1-3H3/t14-/m1/s1
Release date: 2017-06-07
The novel p300/CBP inhibitor A-485 uncovers a unique mechanism of action to target AR in castrate resistant prostate cancer (PDB entry 5KJ2)
Macromolecule: Histone acetyltransferase p300
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.3.1.48
Sequence length: 348 residues
Sequence: KFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDRHLEFSSLRRAQWSTGCMLVELHTQSQDRF
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.95
R work: 0.225
R free: 0.26
Average B factor: 39.78
Crystallization method: VAPOR DIFFUSION
Crystallization temperature (K): 290
Crystal growth procedure: 25% (w/v) PEG3350, 0.2M Sodium Chloride, 0.1M BIS-TRIS buffer pH5.5
Matthews coefficient: 2.61
Solvent content (%): 52.92
Ligand: N-[(4-fluorophenyl)methyl]-2-{(1R)-5-[(methylcarbamoyl)amino]-2',4'-dioxo-2,3-dihydro-3'H-spiro[indene-1,5'-[1,3]oxazolidin]-3'-yl}-N-[(2S)-1,1,1-trifluoropropan-2-yl]acetamide (6TF)
Ligand formula: C25 H24 F4 N4 O5
Ligand molecular weight: 536.475
Ligand SMILES: CC(C(F)(F)F)N(Cc1ccc(cc1)F)C(=O)CN2C(=O)C3(CCc4c3ccc(c4)NC(=O)NC)OC2=O
Ligand InChI: InChI=1S/C25H24F4N4O5/c1-14(25(27,28)29)32(12-15-3-5-17(26)6-4-15)20(34)13-33-21(35)24(38-23(33)37)10-9-16-11-18(7-8-19(16)24)31-22(36)30-2/h3-8,11,14H,9-10,12-13H2,1-2H3,(H2,30,31,36)/t14-,24+/m0/s1
Release date: 2017-09-27
Crystal structure of the complex of human angiotensinogen and renin at 2.55 Angstrom (PDB entry 6I3F)
Macromolecule: Angiotensinogen
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
Sequence length: 458 residues
Sequence: DRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKQCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGSSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDQSTSVSVPMLSGMGTFQHWSDIQDQFSVTQVPFTESASLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTAHHHHHH
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.55
R work: 0.20621
R free: 0.23392
Average B factor: 40.386
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.6
Crystallization temperature (K): 293
Crystal growth procedure: 1.76M Ammonium sulfate
0.1M Tris, pH7.6
Matthews coefficient: 3.3
Solvent content (%): 62.74
Ligand: SULFATE ION (SO4)
Ligand formula: O4 S
Ligand molecular weight: 96.063
Ligand SMILES: [O-]S(=O)(=O)[O-]
Ligand InChI: InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
Release date: 2018-12-26
Structure of compound 4 bound human Phospholipase D2 catalytic domain (PDB entry 6OHQ)
Macromolecule: Phospholipase D2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.4.4
Sequence length: 640 residues
Sequence: SSYRQARWWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRALMLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSESAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQCTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICDDFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQGHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.694
R work: 0.2064
R free: 0.2587
Average B factor: 48.1632
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 298
Crystal growth procedure: 0.2M ammonium sulfate, 20% PEG3350, 0.1M bis-tris pH 6.7
Matthews coefficient: 2.01
Solvent content (%): 38.71
Ligand: 4-fluoro-N-{(2S)-1-[4-(2-oxo-2,3-dihydro-1H-benzimidazol-1-yl)piperidin-1-yl]propan-2-yl}benzamide (MKA)
Ligand formula: C22 H25 F N4 O2
Ligand molecular weight: 396.458
Ligand SMILES: CC(CN1CCC(CC1)N2c3ccccc3NC2=O)NC(=O)c4ccc(cc4)F
Ligand InChI: InChI=1S/C22H25FN4O2/c1-15(24-21(28)16-6-8-17(23)9-7-16)14-26-12-10-18(11-13-26)27-20-5-3-2-4-19(20)25-22(27)29/h2-9,15,18H,10-14H2,1H3,(H,24,28)(H,25,29)/t15-/m0/s1
Release date: 2020-02-19
LINE-1 endonuclease domain complex with DNA (PDB entry 7N8S)
Macromolecule: LINE-1 retrotransposable element ORF2 protein
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.7.49
Sequence length: 238 residues
Sequence: MTGSNSHITILTLNINGLNSAIKRHRLASWIKSQDPSVCCIQETHLTCRDTHRLKIKGWRKIYQANGKQKKAGVAILVSDKTDFKPTKIKRDKEGHYIMVKGSIQQEELTILNIYAPNTGAPRFIKQVLSDLQRDLDSHTLIMGAFNTPLSTLDRSTRQKVNKDTQELNSALHQADLIDIYRTLHPKSTEYTFFSAPHHTYSKIDHIVGSKALLSKCKRTEIITNKLSDHSAIKLELR
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.79
R work: 0.2635
R free: 0.3218
Average B factor: 64.29
Crystallization method: EVAPORATION
Crystallization pH: 4.5
Crystallization temperature (K): 298
Crystal growth procedure: 0.2M NH4 CH3 CO2; 15% PEG 4000
Matthews coefficient: 3.84
Solvent content (%): 67.97
Release date: 2021-10-13
Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with 5-methyl-UTP (PDB entry 5TFG)
Macromolecule: Cystic fibrosis transmembrane conductance regulator
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.6.3.49
Sequence length: 229 residues
Sequence: SLTTTEVVMENVTAFWEEGGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.91
R work: 0.1563
R free: 0.1836
Crystallization method: MICROBATCH
Crystallization temperature (K): 279
Crystal growth procedure: Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5;
Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Matthews coefficient: 2.38
Solvent content (%): 48.26
Ligand: MAGNESIUM ION (MG)
Ligand formula: Mg
Ligand molecular weight: 24.305
Ligand SMILES: [Mg+2]
Ligand InChI: InChI=1S/Mg/q+2
Release date: 2018-05-09
Structure of DYRK1A in complex with complex 10 (PDB entry 7A5B)
Macromolecule: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.12.1
Sequence length: 382 residues
Sequence: MHHHHHHSSGVDLGTENLYFQSMSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADE
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.6
R work: 0.1536
R free: 0.1917
Average B factor: 42.335
Crystallization method: VAPOR DIFFUSION
Crystallization pH: 6.5
Crystallization temperature (K): 293
Crystal growth procedure: 0.1M MES buffer at pH 6.5, 12% Peg3350, 0.2M MgCl2
Matthews coefficient: 2.28
Solvent content (%): 46.08
Ligand: 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine (MFR)
Ligand formula: C12 H11 N5 O
Ligand molecular weight: 241.249
Ligand SMILES: COc1ccnc2c1c(c[nH]2)c3ccnc(n3)N
Ligand InChI: InChI=1S/C12H11N5O/c1-18-9-3-5-14-11-10(9)7(6-16-11)8-2-4-15-12(13)17-8/h2-6H,1H3,(H,14,16)(H2,13,15,17)
Release date: 2021-06-30
Crystal structure of MELK in complex with an inhibitor (PDB entry 5MAF)
Macromolecule: Maternal embryonic leucine zipper kinase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 347 residues
Sequence: GPKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.8
R work: 0.20965
R free: 0.25919
Average B factor: 56.237
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 293
Crystal growth procedure: 10-20% PEG 3350 or PEG 4000, 0.1 M BIS TRIS pH 6.5, 0.6M NaCl
Matthews coefficient: 2.17
Solvent content (%): 43.22
Ligand: DIMETHYL SULFOXIDE (DMS)
Ligand formula: C2 H6 O S
Ligand molecular weight: 78.133
Ligand SMILES: CS(=O)C
Ligand InChI: InChI=1S/C2H6OS/c1-4(2)3/h1-2H3
Release date: 2017-12-06
Crystal structure of INPP5B in complex with biphenyl 3,3',4,4',5,5'- hexakisphosphate (PDB entry 5A7I)
Macromolecule: TYPE II INOSITOL 1,4,5-TRISPHOSPHATE 5-PHOSPHATASE
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.3.36
Sequence length: 313 residues
Sequence: MYTYIQNFRFFAGTYNVNGQSPKECLRLWLSNGIQAPDVYCVGFQELDLSKEAFFFHDTPKEEEWFKAVSEGLHPDAKYAKVKLIRLVGIMLLLYVKQEHAAYISEVEAETVGTGIMGRMGNKGGVAIRFQFHNTSICVVNSHLAAHIEEYERRNQDYKDICSRMQFCQPDPSLPPLTISNHDVILWLGDLNYRIEELDVEKVKKLIEEKDFQMLYAYDQLKIQVAAKTVFEGFTEGELTFQPTYKYDTGSDDWDTSEKCRAPAWCDRILWKGKNITQLSYQSHMALKTSDHKPVSSVFDIGVRVVAHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.89
R work: 0.197
R free: 0.22324
Average B factor: 71.185
Crystallization pH: 6.2
Crystal growth procedure: 10% GLYCEROL, 25% PROPANEDIOL AND 0.1 M SODIUM/POTASSIUM PHOSPHATE PH 6.2
Matthews coefficient: 4.96
Solvent content (%): 75.2
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: 2016-04-13
The crystal structure of CK2alpha in complex with an analogue of compound 22 (PDB entry 5OTP)
Macromolecule: Casein kinase II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 352 residues
Sequence: GSMDIEFDDDADDDGSGSGSGSGSSGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVK
Oligomeric state: Homo 2-mer
Stoichiometry: A2
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.57
R work: 0.222
R free: 0.24
Average B factor: 38.88
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 298
Crystal growth procedure: 112.5mM Mes pH 6.5, 35% glycerol ethoxylate, 180 mM ammonium acetate
Matthews coefficient: 2.25
Solvent content (%): 45.25
Ligand: ACETATE ION (ACT)
Ligand formula: C2 H3 O2
Ligand molecular weight: 59.044
Ligand SMILES: CC(=O)[O-]
Ligand InChI: InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
Release date: 2018-09-05
DYRK1A IN COMPLEX WITH CHLORO BENZOTHIAZOLE FRAGMENT (PDB entry 5A4Q)
Macromolecule: DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE 1A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.12.1
Sequence length: 368 residues
Sequence: GASDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.37
R work: 0.2066
R free: 0.24251
Average B factor: 48.573
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.8
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 M KSCN; 0.1M NACL; 16% PEG 3350, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
Matthews coefficient: 2.65
Solvent content (%): 53.5
Ligand: N-(5-CHLORANYL-1,3-BENZOTHIAZOL-2-YL)ETHANAMIDE (Y3L)
Ligand formula: C9 H7 Cl N2 O S
Ligand molecular weight: 226.683
Ligand SMILES: CC(=O)Nc1nc2ccc(cc2s1)Cl
Ligand InChI: InChI=1S/C9H7ClN2OS/c1-5(13)11-9-12-7-3-2-6(10)4-8(7)14-9/h2-4H,1H3,(H,11,12,13)
Release date: 2016-06-29
Mutant human titin immunoglobulin-like 21 domain - C3575S (PDB entry 8P35)
Macromolecule: Titin
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 100 residues
Sequence: GGTGPIFIKEVSNADISMGDVATLSVTVIGIPKPKIQWFFNGVLLTPSADYKFVFDGDDHSLIILFTKLEDEGEYTSMASNDYGKTICSAYLKINSKGEG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.2
R work: 0.22
R free: 0.25
Average B factor: 42.85
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 M HEPES sodium salt, pH 7.5, 25 %(w/v) PEG 2000 MME
Matthews coefficient: 2.61
Solvent content (%): 52.82
Release date: 2023-11-29
HUMAN CK2 KINASE ALPHA SUBUNIT IN COMPLEX WITH THE ATP-COMPETITIVE INHIBITOR 4-BROMOBENZOTRIAZOLE (PDB entry 6TLW)
Macromolecule: Casein kinase II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 399 residues
Sequence: MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQLEHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.73
R work: 0.1602
R free: 0.1873
Average B factor: 46.655
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 290
Crystal growth procedure: 0.1 M sodium HEPES/MOPS buffer pH 7.5, 20 mM sodium formate, 20 mM ammonium acetate, 20 mM sodium citrate tribasic dihydrate, 20 mM sodium potassium tartrate tetrahydrate, 20 mM sodium oxamate, 20% polyethylene glycol 550 monomethyl ester, 10% polyethylene glycol 20000
Matthews coefficient: 3.16
Solvent content (%): 61.09
Ligand: 7-bromanyl-1~{H}-benzotriazole (NKZ)
Ligand formula: C6 H4 Br N3
Ligand molecular weight: 198.02
Ligand SMILES: c1cc2c(c(c1)Br)[nH]nn2
Ligand InChI: InChI=1S/C6H4BrN3/c7-4-2-1-3-5-6(4)9-10-8-5/h1-3H,(H,8,9,10)
Release date: 2020-12-16
CRYSTAL STRUCTURE OF TYROSINE KINASE 2 JH2 (PSEUDO KINASE DOMAIN) COMPLEXED WITH Compound-6c AKA 6-((1-(4-CYANOPHENY L)-2-OXO-1,2-DIHYDRO-3-PYRIDINYL)AMINO)-N-CYCLOPROPYL-8-(M ETHYLAMINO)IMIDAZO[1,2-B]PYRIDAZINE-3-CARBOXAMIDE (PDB entry 6NSL)
Macromolecule: Non-receptor tyrosine-protein kinase TYK2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 317 residues
Sequence: MGSSHHHHHHSSGETVRFQGHMNLSQLSFHRVDQKEITQLSHLGQGTRTNVYEGRLRVEGSGDPEEGKMDDEDPLVPGRDRGQELRVVLKVLDPSHHDIALAFYETASLMSQVSHTHLAFVHGVCVRGPENIMVTEYVEHGPLDVWLRRERGHVPMAWKMVVAQQLASALSYLENKNLVHGNVCGRNILLARLGLAEGTSPFIKLSDPGVGLGALSREERVERIPWLAPECLPGGANSLSTAMDKWGFGATLLEICFDGEAPLQSRSPSEKEHFYQRQHRLPEPSCPQLATLTSQCLTYEPTQRPSFRTILRDLTRL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.15
R work: 0.202
R free: 0.213
Average B factor: 41.78
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 200 mM ammonium sulfate, and 100 mM sodium cacodylate buffer, pH 6.5, 30%(W/V) PEG 5000 (Methyl Ether)
Matthews coefficient: 1.92
Solvent content (%): 36.13
Ligand: 6-{[1-(4-cyanophenyl)-2-oxo-1,2-dihydropyridin-3-yl]amino}-N-cyclopropyl-8-(methylamino)imidazo[1,2-b]pyridazine-3-carboxamide (KZJ)
Ligand formula: C23 H20 N8 O2
Ligand molecular weight: 440.457
Ligand SMILES: CNc1cc(nn2c1ncc2C(=O)NC3CC3)NC4=CC=CN(C4=O)c5ccc(cc5)C#N
Ligand InChI: InChI=1S/C23H20N8O2/c1-25-18-11-20(29-31-19(13-26-21(18)31)22(32)27-15-6-7-15)28-17-3-2-10-30(23(17)33)16-8-4-14(12-24)5-9-16/h2-5,8-11,13,15,25H,6-7H2,1H3,(H,27,32)(H,28,29)
Release date: 2020-01-29