satarupa22/MacromolecularLigandDB huggingface dataset:
The complex of CCG-257081 bound to pirin (PDB entry 6N0K)
Macromolecule: Pirin
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 1.13.11.24
Sequence length: 301 residues
Sequence: MRGSHHHHHHGSGSSKKVTLSVLSREQSEGVGARVRRSIGRPELKNLDPFLLFDEFKGGRPGGFPDHPHRGFETVSYLLEGGSMAHEDFCGHTGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRSSEKMVEPQYQELKSEEIPKPSKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDPGAKHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDSVQVENKDPKRSHFVLIAGEPLREPVIQHGPFVMNTNEEISQAILDFRNAKNGFERAKTWKSKIGN
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.46
R work: 0.1774
R free: 0.2089
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 295
Crystal growth procedure: 0.1 M Hepes pH 7.5, 8% Ethylene Glycol, 20% PEG 8000
Matthews coefficient: 2.27
Solvent content (%): 45.91
Ligand: FE (III) ION (FE)
Ligand formula: Fe
Ligand molecular weight: 55.845
Ligand SMILES: [Fe+3]
Ligand InChI: InChI=1S/Fe/q+3
Release date: 2019-07-10
ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1273312142 (PDB entry 7G8T)
Macromolecule: Transforming protein RhoA
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.6.5.2
Sequence length: 185 residues
Sequence: SMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRG
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.385
R work: 0.1798
R free: 0.1983
Average B factor: 24.41
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 293
Crystal growth procedure: 100 mM Tris, 2.6M sodium formate
Matthews coefficient: 2.5
Solvent content (%): 50.76
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: 2023-07-12
Crystal Structure of the PTP1B YopH WPD loop Chimera 3 apo form (PDB entry 6XE8)
Macromolecule: Tyrosine-protein phosphatase non-receptor type 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.3.48
Sequence length: 321 residues
Sequence: MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYGNWPDQTAPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHN
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.952
R work: 0.1632
R free: 0.1852
Average B factor: 49.8204
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8.5
Crystallization temperature (K): 277.15
Crystal growth procedure: tris hydrochloride pH 8.5, magnesium acetate tetrahydrate, PEG 8000 and benzamidine
Matthews coefficient: 3.17
Solvent content (%): 59.92
Ligand: BENZAMIDINE (BEN)
Ligand formula: C7 H8 N2
Ligand molecular weight: 120.152
Ligand SMILES: [H]N=C(c1ccccc1)N
Ligand InChI: InChI=1S/C7H8N2/c8-7(9)6-4-2-1-3-5-6/h1-5H,(H3,8,9)
Release date: 2021-12-15
Crystal structure of PML B-box2 (PDB entry 8J2P)
Macromolecule: Maltose/maltodextrin-binding periplasmic protein,Protein PML
Type: Protein, polypeptide(L)
Source organism: Escherichia coli K-12
EC number: 2.3.2
Sequence length: 428 residues
Sequence: MGKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAAAEFKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQR
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.09
R work: 0.1912
R free: 0.2346
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 291
Crystal growth procedure: 20% PEG 3350
Matthews coefficient: 2.61
Solvent content (%): 52.86
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: 2023-09-20
Crystal structure of the human METTL3-METTL14 complex bound to Compound 8 (ASI_M3M_091) (PDB entry 6TU1)
Macromolecule: N6-adenosine-methyltransferase catalytic subunit
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.1.1.348
Sequence length: 580 residues
Sequence: MSDTWSSIQAHKKQLDSLRERLQRRRKQDSGHLDLRNPEAALSPTFRSDSPVPTAPTSGGPKPSTASAVPELATDPELEKKLLHHLSDLALTLPTDAVSICLAISTPDAPATQDGVESLLQKFAAQELIEVKRGLLQDDAHPTLVTYADHSKLSAMMGAVAEKKGPGEVAGTVTGQKRRAEQDSTTVAAFASSLVSGLNSSASEPAKEPAKKSRKHAASDVDLEIESLLNQQSTKEQQSKKVSQEILELLNTTTAKEQSIVEKFRSRGRAQVQEFCDYGTKEECMKASDADRPCRKLHFRRIINKHTDESLGDCSFLNTCFHMDTCKYVHYEIDACMDSEAPGSKDHTPSQELALTQSVGGDSSADRLFPPQWICCDIRYLDVSILGKFAVVMADPPWDIHMELPYGTLTDDEMRRLNIPVLQDDGFLFLWVTGRAMELGRECLNLWGYERVDEIIWVKTNQLQRIIRTGRTGHWLNHGKEHCLVGVKGNPQGFNQGLDCDVIVAEVRSTSHKPDEIYGMIERLSPGTRKIELFGRPHNVQPNWITLGNQLDGIHLLDPDVVARFKQRYPDGIISKPKNL
Oligomeric state: Hetero 2-mer
Stoichiometry: A1, B1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.31
R work: 0.1949
R free: 0.2339
Average B factor: 46.39
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 295
Crystal growth procedure: 25% PEG 3350, 200 mM Magnesium acetate
Ligand: (2~{R},3~{R},4~{R},5~{R})-2-[(6-aminopurin-9-yl)methyl]-5-azanyl-oxane-3,4-diol (NXB)
Ligand formula: C11 H16 N6 O3
Ligand molecular weight: 280.283
Ligand SMILES: c1nc(c2c(n1)n(cn2)CC3C(C(C(CO3)N)O)O)N
Ligand InChI: InChI=1S/C11H16N6O3/c12-5-2-20-6(9(19)8(5)18)1-17-4-16-7-10(13)14-3-15-11(7)17/h3-6,8-9,18-19H,1-2,12H2,(H2,13,14,15)/t5-,6-,8-,9+/m1/s1
Release date: 2020-03-04
Crystal structure of human secreted phospholipase A2 group IIE with Compound 8 (PDB entry 5WZS)
Macromolecule: Group IIE secretory phospholipase A2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.1.4
Sequence length: 123 residues
Sequence: NLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDWCCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNLGTYNRKYAHYPNKLCTGPTPPC
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.3
R work: 0.215
R free: 0.2655
Average B factor: 30.86
Crystallization method: VAPOR DIFFUSION
Crystallization temperature (K): 277
Crystal growth procedure: 2.2 M Sodium chloride, 0.1 M BIS-TRIS propane pH 7.0
Matthews coefficient: 3.38
Solvent content (%): 63.63
Ligand: 2-[2-methyl-1-(naphthalen-1-ylmethyl)-3-oxamoyl-indol-4-yl]oxyethanoic acid (7W9)
Ligand formula: C24 H20 N2 O5
Ligand molecular weight: 416.426
Ligand SMILES: Cc1c(c2c(n1Cc3cccc4c3cccc4)cccc2OCC(=O)O)C(=O)C(=O)N
Ligand InChI: InChI=1S/C24H20N2O5/c1-14-21(23(29)24(25)30)22-18(10-5-11-19(22)31-13-20(27)28)26(14)12-16-8-4-7-15-6-2-3-9-17(15)16/h2-11H,12-13H2,1H3,(H2,25,30)(H,27,28)
Release date: 2018-01-24
Human Carbonic anhydrase II bound by napthalene-1-sulfonamide (PDB entry 6T4P)
Macromolecule: carbonic anhydrase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.1
Sequence length: 260 residues
Sequence: MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.75
R work: 0.1615
R free: 0.1993
Average B factor: 16.051
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 291
Crystal growth procedure: Crystallization buffer was 0.1M sodium BICINE, pH 9, and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
Matthews coefficient: 2.06
Solvent content (%): 40.17
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: 2020-10-14
Human carbonic anhydrase II with bound IrCp* complex (cofactor 7) to generate an artificial transfer hydrogenase (ATHase) (PDB entry 6QFU)
Macromolecule: Carbonic anhydrase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.1
Sequence length: 260 residues
Sequence: MAHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.8
R work: 0.1649
R free: 0.1864
Average B factor: 17.635
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.9
Crystallization temperature (K): 293
Crystal growth procedure: 2.6 M ammonium sulfate, 50 mM Tris-H2SO4
Matthews coefficient: 2.1
Solvent content (%): 41.38
Ligand: 4-[2-(9-chloranyl-2',3',4',5',6'-pentamethyl-4-oxidanyl-7-oxidanylidene-spiro[1$l^{4},8-diaza-9$l^{8}-iridabicyclo[4.3.0]nona-1(6),2,4-triene-9,1'-1$l^{8}-iridapentacyclo[2.2.0.0^{1,3}.0^{1,5}.0^{2,6}]hexane]-8-yl)ethyl]benzenesulfonamide (J0K)
Ligand formula: C24 H29 Cl Ir N3 O4 S
Ligand molecular weight: 683.24
Ligand SMILES: CC12C3([Ir]1456(C2(C4(C53C)C)C)([N]7=C(C=C(C=C7)O)C(=O)N6CCc8ccc(cc8)S(=O)(=O)N)Cl)C
Ligand InChI: InChI=1S/C14H15N3O4S.C10H15.ClH.Ir/c15-22(20,21)12-3-1-10(2-4-12)5-7-17-14(19)13-9-11(18)6-8-16-13;1-6-7(2)9(4)10(5)8(6)3;;/h1-4,6,8-9H,5,7H2,(H4,15,16,17,18,19,20,21);1-5H3;1H;/q;;;+2/p-2
Release date: 2019-04-17
Pak1 in complex with 7-azaindole inhibitor (PDB entry 5KBR)
Macromolecule: Serine/threonine-protein kinase PAK 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 289 residues
Sequence: LEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRNIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSEMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLDMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.36
R work: 0.195
R free: 0.255
Average B factor: 91.42
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.6
Crystallization temperature (K): 293
Crystal growth procedure: 0.2M ammonium sulphate, 16% PEG 3350, 0.1M Hepes (pH 7.6)
Matthews coefficient: 2.46
Solvent content (%): 50.1
Ligand: (4-chlorophenyl)-[5-(1-piperidin-4-ylpyrazol-4-yl)-1~{H}-pyrrolo[2,3-b]pyridin-3-yl]methanone (IPW)
Ligand formula: C22 H20 Cl N5 O
Ligand molecular weight: 405.88
Ligand SMILES: c1cc(ccc1C(=O)c2c[nH]c3c2cc(cn3)c4cnn(c4)C5CCNCC5)Cl
Ligand InChI: InChI=1S/C22H20ClN5O/c23-17-3-1-14(2-4-17)21(29)20-12-26-22-19(20)9-15(10-25-22)16-11-27-28(13-16)18-5-7-24-8-6-18/h1-4,9-13,18,24H,5-8H2,(H,25,26)
Release date: 2016-09-28
Crystal Structure of human PARP-1 ART domain bound to inhibitor UTT93 (PDB entry 6NRJ)
Macromolecule: Poly [ADP-ribose] polymerase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.4.2.30
Sequence length: 271 residues
Sequence: MGSSHHHHHHSSGLVPRGSHMTKSKLPKPVQDLIKMIFGSGSGSGGDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.65
R work: 0.1677
R free: 0.1913
Average B factor: 34.032
Crystallization method: EVAPORATION
Crystallization pH: 7.5
Crystallization temperature (K): 298
Crystal growth procedure: ~20% PEG 3350, 0.2 M ammonium sulfate or sodium citrate, 100 mM Hepes pH 7.5
Matthews coefficient: 2.56
Solvent content (%): 51.92
Ligand: (2Z)-2-[(4-{[2-(1H-benzimidazol-2-yl)ethyl]carbamoyl}phenyl)methylidene]-3-oxo-2,3-dihydro-1-benzofuran-7-carboxamide (KYJ)
Ligand formula: C26 H20 N4 O4
Ligand molecular weight: 452.461
Ligand SMILES: c1ccc2c(c1)[nH]c(n2)CCNC(=O)c3ccc(cc3)C=C4C(=O)c5cccc(c5O4)C(=O)N
Ligand InChI: InChI=1S/C26H20N4O4/c27-25(32)18-5-3-4-17-23(31)21(34-24(17)18)14-15-8-10-16(11-9-15)26(33)28-13-12-22-29-19-6-1-2-7-20(19)30-22/h1-11,14H,12-13H2,(H2,27,32)(H,28,33)(H,29,30)/b21-14-
Release date: 2019-08-14
KRas G12C in complex with Compound 5c (PDB entry 7YCC)
Macromolecule: Isoform 2B of GTPase KRas
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.6.5.2
Sequence length: 170 residues
Sequence: GMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.79
R work: 0.2116
R free: 0.255
Average B factor: 35.302
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 293
Crystal growth procedure: MES, ammonium sulfate, PEG550MME
Matthews coefficient: 2.64
Solvent content (%): 53.35
Ligand: GUANOSINE-5'-DIPHOSPHATE (GDP)
Ligand formula: C10 H15 N5 O11 P2
Ligand molecular weight: 443.201
Ligand SMILES: c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
Ligand InChI: InChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
Release date: 2022-08-10
Covalent fragment group deposition -- Crystal Structure of OUTB2 in complex with PCM-0102998 (PDB entry 5QIV)
Macromolecule: Ubiquitin thioesterase OTUB2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.19.12
Sequence length: 225 residues
Sequence: FNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDRNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYNILYA
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.39
R work: 0.1365
R free: 0.1838
Average B factor: 19.971
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7
Crystallization temperature (K): 293
Crystal growth procedure: 16% PEG4K, 0.1M HEPES pH 7.0, 8% 2-propanol, 5 mM DTT
Matthews coefficient: 2.35
Solvent content (%): 47.6
Ligand: 1,2-ETHANEDIOL (EDO)
Ligand formula: C2 H6 O2
Ligand molecular weight: 62.068
Ligand SMILES: C(CO)O
Ligand InChI: InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
Release date: 2019-12-18
ATAD2 in complex with FragLite33 (PDB entry 7R00)
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): 1.48
R work: 0.2067
R free: 0.2367
Average B factor: 32.147
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 293
Crystal growth procedure: 0.1M BisTris pH 6-7, 1.7-2.1M Ammonium sulphate
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: 2022-12-07
DYRK1A bound to a harmine derivative (PDB entry 6UWY)
Macromolecule: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.12.1
Sequence length: 361 residues
Sequence: SMSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADE
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.95
R work: 0.1951
R free: 0.2271
Average B factor: 98.726
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 8.8
Crystallization temperature (K): 277
Crystal growth procedure: 35-45% PEG400, 0.2 M lithium sulfate, 0.1 M Tris, pH 8.8
Matthews coefficient: 3.22
Solvent content (%): 61.8
Ligand: 4-(7-methoxy-1-methyl-9H-beta-carbolin-9-yl)butanamide (QKG)
Ligand formula: C17 H19 N3 O2
Ligand molecular weight: 297.352
Ligand SMILES: Cc1c2c(ccn1)c3ccc(cc3n2CCCC(=O)N)OC
Ligand InChI: InChI=1S/C17H19N3O2/c1-11-17-14(7-8-19-11)13-6-5-12(22-2)10-15(13)20(17)9-3-4-16(18)21/h5-8,10H,3-4,9H2,1-2H3,(H2,18,21)
Release date: 2020-02-12
Mimic carbonic anhydrase IX in complex with Methyl 2-chloro-4-(cyclohexylsulfanyl)-5-sulfamoylbenzoate (PDB entry 7Q0C)
Macromolecule: Carbonic anhydrase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.1
Sequence length: 260 residues
Sequence: MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVEFDDSQDKAVLKGGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKALQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.12
R work: 0.1603
R free: 0.1937
Average B factor: 18.286
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 291
Crystal growth procedure: Crystallization buffer: 0.1M sodium bicine (pH 9.0), 0.2 M ammonium sulfate and 2M sodium malonate (pH 7.0)
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: 2022-01-12
CRYSTAL STRUCTURE OF IRAK-4 WITH A 4,6-DIAMINONICOTINAMIDE INHIBITOR (COMPOUND NUMBER 4) (PDB entry 5W84)
Macromolecule: Interleukin-1 receptor-associated kinase 4
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 305 residues
Sequence: GAMGVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.9
R work: 0.2
R free: 0.248
Average B factor: 83.58
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: Null
Matthews coefficient: 2.85
Solvent content (%): 56.88
Ligand: 4-(benzylamino)-6-[(2-oxo-2,3-dihydro-1H-indol-5-yl)amino]pyridine-3-carboxamide (9YY)
Ligand formula: C21 H19 N5 O2
Ligand molecular weight: 373.408
Ligand SMILES: c1ccc(cc1)CNc2cc(ncc2C(=O)N)Nc3ccc4c(c3)CC(=O)N4
Ligand InChI: InChI=1S/C21H19N5O2/c22-21(28)16-12-24-19(10-18(16)23-11-13-4-2-1-3-5-13)25-15-6-7-17-14(8-15)9-20(27)26-17/h1-8,10,12H,9,11H2,(H2,22,28)(H,26,27)(H2,23,24,25)
Release date: 2017-10-11
Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in complex with AZ8838 at 2.8 angstrom resolution (PDB entry 5NDD)
Macromolecule: Lysozyme,Proteinase-activated receptor 2,Soluble cytochrome b562,Proteinase-activated receptor 2
Type: Protein, polypeptide(L)
Source organism: Tequatrovirus T4
EC number: 3.2.1.17
Sequence length: 619 residues
Sequence: MVSAIVLYVLLAAAAHSAFAAASNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYIYEFFSVDEFSASVLTGKLTTVFLPIVYTIVFVVALPSNGMALWVFLFRTKKKAPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYANMYCSILFLTCLSVQRAWEIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALQITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRALADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLENSEKKRKRAIKLAVTVAAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKAAAHHHHHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.801
R work: 0.2224
R free: 0.2639
Crystallization method: LIPIDIC CUBIC PHASE
Crystallization pH: 5.8
Crystallization temperature (K): 293
Crystal growth procedure: 0.1 M sodium citrate/citrate acid pH 5.5-6.2, 0.2 M ammonium phosphate dibasic, 38-43 % (w/v) PEG400 and 1 mM AZ8838
Matthews coefficient: 3.04
Solvent content (%): 59.52
Ligand: (~{S})-(4-fluoranyl-2-propyl-phenyl)-(1~{H}-imidazol-2-yl)methanol (8TZ)
Ligand formula: C13 H15 F N2 O
Ligand molecular weight: 234.269
Ligand SMILES: CCCc1cc(ccc1C(c2[nH]ccn2)O)F
Ligand InChI: InChI=1S/C13H15FN2O/c1-2-3-9-8-10(14)4-5-11(9)12(17)13-15-6-7-16-13/h4-8,12,17H,2-3H2,1H3,(H,15,16)/t12-/m0/s1
Release date: 2017-05-03
CRYSTAL STRUCTURE OF HUMAN WEE1 KINASE DOMAIN IN COMPLEX WITH RAC-IV-016, a MK1775 analougue (PDB entry 5VD4)
Macromolecule: Wee1-like protein kinase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 289 residues
Sequence: GAGSMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.02
R work: 0.2026
R free: 0.2453
Average B factor: 44.9582
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6.9
Crystallization temperature (K): 291
Crystal growth procedure: 5.0 MG/ML WEE1, 25 mM Na/K phosphate, 1 mM DTT, 0.05 M ammonium sulfate, 0.05 M Bis-tris (pH 5.5), 7.5 % PEG 3350, 1 mM RAC-IV-016
Matthews coefficient: 2.15
Solvent content (%): 42.66
Ligand: 6-{[4-(4-methylpiperazin-1-yl)phenyl]amino}-2-(prop-2-en-1-yl)-1-{6-[(1S)-2,2,2-trifluoro-1-hydroxyethyl]pyridin-2-yl}-1,2-dihydro-3H-pyrazolo[3,4-d]pyrimidin-3-one (99J)
Ligand formula: C26 H27 F3 N8 O2
Ligand molecular weight: 540.54
Ligand SMILES: CN1CCN(CC1)c2ccc(cc2)Nc3ncc4c(n3)N(N(C4=O)CC=C)c5cccc(n5)C(C(F)(F)F)O
Ligand InChI: InChI=1S/C26H27F3N8O2/c1-3-11-36-24(39)19-16-30-25(31-17-7-9-18(10-8-17)35-14-12-34(2)13-15-35)33-23(19)37(36)21-6-4-5-20(32-21)22(38)26(27,28)29/h3-10,16,22,38H,1,11-15H2,2H3,(H,30,31,33)/t22-/m0/s1
Release date: 2018-04-04
Crystal structure of human carbonic anhydrase II in complex with the 4-(3-aminophenyl)benzenesulfonamide inhibitor (PDB entry 5E2K)
Macromolecule: Carbonic anhydrase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 4.2.1.1
Sequence length: 257 residues
Sequence: HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.4
R work: 0.1677
R free: 0.1931
Average B factor: 13.924
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8
Crystallization temperature (K): 296
Crystal growth procedure: 1.5 M sodium citrate, Tris 50 mM
Matthews coefficient: 2.12
Solvent content (%): 41.9
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: 2016-01-20