satarupa22/MacromolecularLigandDB huggingface dataset:
CHK1 KINASE IN COMPLEX WITH COMPOUND 13 (PDB entry 6FCK)
Macromolecule: Serine/threonine-protein kinase Chk1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 276 residues
Sequence: MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRP
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.9
R work: 0.174
R free: 0.214
Average B factor: 21.7
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 298
Crystal growth procedure: 16% Peg8k, 0.1M Caco pH 6.8, 0.15M AS
Matthews coefficient: 2.42
Solvent content (%): 49.1
Ligand: 2-phenyl-4-[[(3~{S})-piperidin-3-yl]amino]-1~{H}-indole-7-carboxamide (D4Z)
Ligand formula: C20 H22 N4 O
Ligand molecular weight: 334.415
Ligand SMILES: c1ccc(cc1)c2cc3c(ccc(c3[nH]2)C(=O)N)NC4CCCNC4
Ligand InChI: InChI=1S/C20H22N4O/c21-20(25)15-8-9-17(23-14-7-4-10-22-12-14)16-11-18(24-19(15)16)13-5-2-1-3-6-13/h1-3,5-6,8-9,11,14,22-24H,4,7,10,12H2,(H2,21,25)/t14-/m0/s1
Release date: 2018-01-17
The crystal structure of CK2alpha in complex with compound 31 (PDB entry 5OYF)
Macromolecule: Casein kinase II subunit alpha
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 342 residues
Sequence: SGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVAAAKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKREAMEHPYFYTVVK
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.54
R work: 0.185
R free: 0.216
Average B factor: 30.35
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: 1.98
Solvent content (%): 37.81
Ligand: 2-(1~{H}-benzimidazol-2-yl)-~{N}-[[4-(2-ethylphenyl)-3-methyl-phenyl]methyl]ethanamine (B4Q)
Ligand formula: C25 H27 N3
Ligand molecular weight: 369.502
Ligand SMILES: CCc1ccccc1c2ccc(cc2C)CNCCc3[nH]c4ccccc4n3
Ligand InChI: InChI=1S/C25H27N3/c1-3-20-8-4-5-9-22(20)21-13-12-19(16-18(21)2)17-26-15-14-25-27-23-10-6-7-11-24(23)28-25/h4-13,16,26H,3,14-15,17H2,1-2H3,(H,27,28)
Release date: 2018-02-28
FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH 4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide (PDB entry 6YVY)
Macromolecule: Focal adhesion kinase 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.2
Sequence length: 282 residues
Sequence: GSGSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEE
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.918
R work: 0.2141
R free: 0.2353
Average B factor: 39.24
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 294
Crystal growth procedure: 15% PEG 3350
Matthews coefficient: 2.82
Solvent content (%): 56.34
Ligand: 4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide (P1E)
Ligand formula: C19 H25 F3 N6 O2 S
Ligand molecular weight: 458.501
Ligand SMILES: CNS(=O)(=O)c1ccc(cc1)Nc2ncc(c(n2)NC3CCCC3N(C)C)C(F)(F)F
Ligand InChI: InChI=1S/C19H25F3N6O2S/c1-23-31(29,30)13-9-7-12(8-10-13)25-18-24-11-14(19(20,21)22)17(27-18)26-15-5-4-6-16(15)28(2)3/h7-11,15-16,23H,4-6H2,1-3H3,(H2,24,25,26,27)/t15-,16-/m1/s1
Release date: 2021-02-10
Pim1 Kinase in complex with a benzofuranone inhibitor (PDB entry 5VUB)
Macromolecule: Serine/threonine-protein kinase pim-1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.1
Sequence length: 298 residues
Sequence: MKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSKSGPSSGENLYFQ
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.0
R work: 0.1603
R free: 0.1837
Average B factor: 32.39
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 5.5
Crystallization temperature (K): 293
Crystal growth procedure: 100MM CITRATE BUFFER, PH 5.5, 200MM      NACL, 1M NH4HPO4
Matthews coefficient: 3.27
Solvent content (%): 62.43
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: 2017-12-13
Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 2e (PDB entry 5NK9)
Macromolecule: Ephrin type-A receptor 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.10.1
Sequence length: 306 residues
Sequence: GDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.588
R work: 0.1621
R free: 0.1945
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 6.5
Crystallization temperature (K): 291
Crystal growth procedure: 37.5% MPD/PEG1000/PEG3350 (MD), 0.1 M Amino Acids Mix (MD), 0.1 M Hepes pH6.5
Matthews coefficient: 1.96
Solvent content (%): 37.36
Ligand: (2~{Z})-~{N}-(2-chloranyl-6-methyl-phenyl)-2-[3-[(4-methyl-4-oxidanyl-cyclohexyl)carbamoyl]phenyl]imino-1,3-thiazolidine-5-carboxamide (912)
Ligand formula: C25 H29 Cl N4 O3 S
Ligand molecular weight: 501.041
Ligand SMILES: Cc1cccc(c1NC(=O)C2CNC(=Nc3cccc(c3)C(=O)NC4CCC(CC4)(C)O)S2)Cl
Ligand InChI: InChI=1S/C25H29ClN4O3S/c1-15-5-3-8-19(26)21(15)30-23(32)20-14-27-24(34-20)29-18-7-4-6-16(13-18)22(31)28-17-9-11-25(2,33)12-10-17/h3-8,13,17,20,33H,9-12,14H2,1-2H3,(H,27,29)(H,28,31)(H,30,32)/t17-,20-,25-/m1/s1
Release date: 2017-06-07
human carbonic anhydrase II in complex with ligand (PDB entry 5EHV)
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): 1.208
R work: 0.1532
R free: 0.1746
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization temperature (K): 280
Crystal growth procedure: ammonium sulfate, tris-chloride
Matthews coefficient: 2.08
Solvent content (%): 40.81
Ligand: (~{E})-3-[3-[[3-(2-hydroxy-2-oxoethyl)phenyl]methoxy]phenyl]prop-2-enoic acid (5ON)
Ligand formula: C18 H16 O5
Ligand molecular weight: 312.317
Ligand SMILES: c1cc(cc(c1)COc2cccc(c2)C=CC(=O)O)CC(=O)O
Ligand InChI: InChI=1S/C18H16O5/c19-17(20)8-7-13-3-2-6-16(10-13)23-12-15-5-1-4-14(9-15)11-18(21)22/h1-10H,11-12H2,(H,19,20)(H,21,22)/b8-7+
Release date: 2016-03-09
CRYSTAL STRUCTURE OF PI3K DELTA IN COMPLEX WITH A TRIFLUORO-ETHYL-PYRAZOL-PYROLOTRIAZINE INHIBITOR (PDB entry 5VLR)
Macromolecule: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.1.153
Sequence length: 1013 residues
Sequence: NQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKT
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.8
R work: 0.208
R free: 0.279
Average B factor: 87.32
Crystallization method: VAPOR DIFFUSION
Crystallization temperature (K): 300
Crystal growth procedure: NULL, VAPOR DIFFUSION, TEMPERATURE
 293K
Matthews coefficient: 2.6
Solvent content (%): 53.2
Ligand: 4-acetyl-1-(3-{4-amino-5-[1-(2,2,2-trifluoroethyl)-1H-pyrazol-5-yl]pyrrolo[2,1-f][1,2,4]triazin-7-yl}phenyl)-3,3-dimethylpiperazin-2-one (9EM)
Ligand formula: C25 H25 F3 N8 O2
Ligand molecular weight: 526.514
Ligand SMILES: CC(=O)N1CCN(C(=O)C1(C)C)c2cccc(c2)c3cc(c4n3ncnc4N)c5ccnn5CC(F)(F)F
Ligand InChI: InChI=1S/C25H25F3N8O2/c1-15(37)34-10-9-33(23(38)24(34,2)3)17-6-4-5-16(11-17)20-12-18(21-22(29)30-14-32-36(20)21)19-7-8-31-35(19)13-25(26,27)28/h4-8,11-12,14H,9-10,13H2,1-3H3,(H2,29,30,32)
Release date: 2017-06-07
PanDDA analysis group deposition -- Crystal Structure of human NUDT22 in complex with N13688a (PDB entry 5R56)
Macromolecule: Uridine diphosphate glucose pyrophosphatase NUDT22
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.6.1.45
Sequence length: 304 residues
Sequence: SMDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVRRLPETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.51
R work: 0.1839
R free: 0.2156
Average B factor: 24.013
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 277
Crystal growth procedure: 0.1M HEPES pH 7.5, 0.3M sodium/potassium phosphate, 15% PEG Smear High, 20% ethylene glycol
Matthews coefficient: 2.01
Solvent content (%): 38.94
Ligand: 2-(2,4-dimethylphenoxy)-1-morpholin-4-yl-ethanone (S07)
Ligand formula: C14 H19 N O3
Ligand molecular weight: 249.306
Ligand SMILES: Cc1ccc(c(c1)C)OCC(=O)N2CCOCC2
Ligand InChI: InChI=1S/C14H19NO3/c1-11-3-4-13(12(2)9-11)18-10-14(16)15-5-7-17-8-6-15/h3-4,9H,5-8,10H2,1-2H3
Release date: 2020-07-01
Human Carbonic Anhydrase II complexed with an inhibitor with a benzenesulfonamide group (3). (PDB entry 4YXO)
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): 1.06
R work: 0.1486
R free: 0.164
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.8
Crystallization temperature (K): 291
Crystal growth procedure: 2.5 uL of the protein solution (10 mg/ml hCAII in 50 mM Tris pH 7.8) were mixed with 2.5 uL of the well solution (2.7 M (NH4)SO4, 100 mM Tris, pH 7.8, saturated with p-chloromercurybenzoicacid) and placed as a hanging drop. Crystals appeared after several days. The crystals were soaked in 3.0 M (NH4)SO4, 100 mM Tris, pH 7.8, saturated with the inhibitor, for 1 day.
Matthews coefficient: 2.08
Solvent content (%): 40.75
Ligand: MERCURIBENZOIC ACID (MBO)
Ligand formula: C7 H5 Hg O2
Ligand molecular weight: 321.703
Ligand SMILES: c1cc(ccc1C(=O)O)[Hg]
Ligand InChI: InChI=1S/C7H5O2.Hg/c8-7(9)6-4-2-1-3-5-6;/h2-5H,(H,8,9);
Release date: 2016-02-03
Crystal structure of human GPX4-U46C-R152H in complex with CDS9 (PDB entry 7U4I)
Macromolecule: Phospholipid hydroperoxide glutathione peroxidase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 1.11.1.12
Sequence length: 192 residues
Sequence: MGSSHHHHHHSSGLVPRGSHMLEAASRDDWRCARSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKHYGPMEEPLVIEKDLPHYF
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.97
R work: 0.2007
R free: 0.2458
Average B factor: 31.7419
Crystallization method: MICROBATCH
Crystallization pH: 7
Crystallization temperature (K): 291
Crystal growth procedure: 0.2 M potassium thiocyanate and 20% (w/v) PEG 3350
Matthews coefficient: 2.18
Solvent content (%): 43.47
Ligand: 2-bromo-N-[(thiophen-2-yl)methyl]acetamide (L9U)
Ligand formula: C7 H8 Br N O S
Ligand molecular weight: 234.114
Ligand SMILES: c1cc(sc1)CNC(=O)CBr
Ligand InChI: InChI=1S/C7H8BrNOS/c8-4-7(10)9-5-6-2-1-3-11-6/h1-3H,4-5H2,(H,9,10)
Release date: 2022-12-07
The extra-helical binding site of GPR40 and the structural basis for allosteric agonism and incretin stimulation (PDB entry 5KW2)
Macromolecule: Free fatty acid receptor 1,Lysozyme,Free fatty acid receptor 1
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.2.1.17
Sequence length: 491 residues
Sequence: MDYKDDDDKGSATMDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSAVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFAPLYAGGGFLAALSAARYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCFVGCLRALARGSNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYGSLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQKAENLYFQGHHHHHHHH
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.76
R work: 0.2304
R free: 0.2727
Average B factor: 41.374
Crystallization method: LIPIDIC CUBIC PHASE
Crystallization temperature (K): 298
Crystal growth procedure: 0.1 M Tris HCl, pH 8.5, 30% PEG 400, 0.2 M ammonium formate.
Matthews coefficient: 3.12
Solvent content (%): 60.54
Ligand: (3~{S})-3-cyclopropyl-3-[2-[1-[2-[2,2-dimethylpropyl-(6-methylpyridin-2-yl)carbamoyl]-5-methoxy-phenyl]piperidin-4-yl]-1-benzofuran-6-yl]propanoic acid (6XQ)
Ligand formula: C38 H45 N3 O5
Ligand molecular weight: 623.781
Ligand SMILES: Cc1cccc(n1)N(CC(C)(C)C)C(=O)c2ccc(cc2N3CCC(CC3)c4cc5ccc(cc5o4)C(CC(=O)O)C6CC6)OC
Ligand InChI: InChI=1S/C38H45N3O5/c1-24-7-6-8-35(39-24)41(23-38(2,3)4)37(44)30-14-13-29(45-5)21-32(30)40-17-15-26(16-18-40)33-20-28-12-11-27(19-34(28)46-33)31(22-36(42)43)25-9-10-25/h6-8,11-14,19-21,25-26,31H,9-10,15-18,22-23H2,1-5H3,(H,42,43)/t31-/m0/s1
Release date: 2018-05-02
Crystal Structure of human phosphodiesterase 10 in complex with 6-cyclopropyl-N-[2-[2-(methylamino)-2-oxoethyl]phenyl]-3-(pyrimidin-5-ylamino)pyridine-2-carboxamide (PDB entry 5SKJ)
Macromolecule: cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.1.4.17
Sequence length: 343 residues
Sequence: GSSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 2.74
R work: 0.166
R free: 0.2489
Average B factor: 45.162
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 7.5
Crystallization temperature (K): 295
Crystal growth procedure: 5-20 mg/mL protein in 25mM HEPES/NaOH pH7.5, 150mM NaCl, 50mM BME mixed 1:1 with reservoir 0.1M HEPES/NaOH pH7.5, 30% PEG550MME, 50mM MgCl2
Matthews coefficient: 2.6
Solvent content (%): 52.74
Ligand: 6-cyclopropyl-N-{2-[2-(methylamino)-2-oxoethyl]phenyl}-3-[(pyrimidin-5-yl)amino]pyridine-2-carboxamide (KG3)
Ligand formula: C22 H22 N6 O2
Ligand molecular weight: 402.449
Ligand SMILES: CNC(=O)Cc1ccccc1NC(=O)c2c(ccc(n2)C3CC3)Nc4cncnc4
Ligand InChI: InChI=1S/C22H22N6O2/c1-23-20(29)10-15-4-2-3-5-17(15)28-22(30)21-19(26-16-11-24-13-25-12-16)9-8-18(27-21)14-6-7-14/h2-5,8-9,11-14,26H,6-7,10H2,1H3,(H,23,29)(H,28,30)
Release date: 2022-10-12
DYRK1A complex with DYR530 (PDB entry 8T2H)
Macromolecule: Dual specificity tyrosine-phosphorylation-regulated kinase 1A
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 2.7.11.23
Sequence length: 365 residues
Sequence: DSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTS
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.85
R work: 0.16329
R free: 0.21303
Average B factor: 21.451
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 6
Crystallization temperature (K): 298
Crystal growth procedure: 1.8 M sodium malonate, 1.3% PEG 400
Matthews coefficient: 2.27
Solvent content (%): 45.86
Ligand: (4P)-4-{(3M)-3-[3-fluoro-4-(4-methylpiperazin-1-yl)phenyl]-2-methyl-3H-imidazo[4,5-b]pyridin-5-yl}pyridin-2-amine (XIR)
Ligand formula: C23 H24 F N7
Ligand molecular weight: 417.482
Ligand SMILES: Cc1nc2ccc(nc2n1c3ccc(c(c3)F)N4CCN(CC4)C)c5ccnc(c5)N
Ligand InChI: InChI=1S/C23H24FN7/c1-15-27-20-5-4-19(16-7-8-26-22(25)13-16)28-23(20)31(15)17-3-6-21(18(24)14-17)30-11-9-29(2)10-12-30/h3-8,13-14H,9-12H2,1-2H3,(H2,25,26)
Release date: 2024-05-15
Carbonic Anhydrase II in complex with 3-ureido benzenesulfonamide derivative (PDB entry 7RNY)
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): 1.29
R work: 0.154
R free: 0.174
Average B factor: 12.871
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization pH: 7.8
Crystallization temperature (K): 293
Crystal growth procedure: 1.6 M sodium citrate, 50 mM tris base
Matthews coefficient: 2.09
Solvent content (%): 41.06
Ligand: 3-{[benzyl(methyl)carbamoyl]amino}benzene-1-sulfonamide (65M)
Ligand formula: C15 H17 N3 O3 S
Ligand molecular weight: 319.379
Ligand SMILES: CN(Cc1ccccc1)C(=O)Nc2cccc(c2)S(=O)(=O)N
Ligand InChI: InChI=1S/C15H17N3O3S/c1-18(11-12-6-3-2-4-7-12)15(19)17-13-8-5-9-14(10-13)22(16,20)21/h2-10H,11H2,1H3,(H,17,19)(H2,16,20,21)
Release date: 2022-06-08
Structure of human methionine aminopeptidase-2 complexed with spiroepoxytriazole inhibitor (+)-31a (PDB entry 5CLS)
Macromolecule: Methionine aminopeptidase 2
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.11.18
Sequence length: 371 residues
Sequence: GPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.75
R work: 0.16001
R free: 0.18885
Average B factor: 22.373
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 5.4
Crystallization temperature (K): 292
Crystal growth procedure: Na Citrate, Tert-butanol
Matthews coefficient: 2.74
Solvent content (%): 55.08
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: 2016-01-13
Crystal structure of Human Carbonic Anhydrase II in complex with the anticonvulsant sulfamide JNJ-26990990 and its S,S-dioxide analog. (PDB entry 5FDC)
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: 0.17
R free: 0.204
Crystallization method: VAPOR DIFFUSION, HANGING DROP
Crystallization temperature (K): 293
Crystal growth procedure: 2.5 M ammonium sulphate, 0.3 M sodium chloride, 0.1 M Tris-HCl, pH 8.4 and 5 mM 4-(hydroxymercurybenzoate)
Matthews coefficient: 2.08
Solvent content (%): 40.81
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: 2016-05-18
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH (PDB entry 5LAB)
Macromolecule: Macrophage metalloelastase
Type: Protein, polypeptide(L)
Source organism: Homo sapiens
EC number: 3.4.24.65
Sequence length: 159 residues
Sequence: MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG
Oligomeric state: Monomer
Stoichiometry: A1
Experimental method: X-RAY DIFFRACTION
Refinement resolution (Å): 1.34
R work: 0.15515
R free: 0.1945
Average B factor: 21.754
Crystallization method: VAPOR DIFFUSION, SITTING DROP
Crystallization pH: 8
Crystallization temperature (K): 293
Crystal growth procedure: Tris, PEG6000, NNGH, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Matthews coefficient: 2.26
Solvent content (%): 45.26
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: 2016-08-10