Structure of PDB 5vwo Chain C Binding Site BS01

Receptor Information
>5vwo Chain C (length=404) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSY
SAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHK
VLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAI
SSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE
AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRP
DIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIA
ALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKET
KDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT
ILSF
Ligand information
Ligand ID9QJ
InChIInChI=1S/C14H19N2O7P/c1-7-13(17)11(10(5-16-7)6-23-24(20,21)22)3-8-2-9(14(18)19)4-12(8)15/h5,8-9,15,17H,2-4,6H2,1H3,(H,18,19)(H2,20,21,22)/b15-12+/t8-,9-/m0/s1
InChIKeyCTOWFYUCLIAQOJ-QEPOKVMRSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Cc1ncc(CO[P](O)(O)=O)c(C[CH]2C[CH](CC2=N)C(O)=O)c1O
OpenEye OEToolkits 2.0.6[H]/N=C/1\C[C@H](C[C@H]1Cc2c(cnc(c2O)C)COP(=O)(O)O)C(=O)O
CACTVS 3.385Cc1ncc(CO[P](O)(O)=O)c(C[C@@H]2C[C@@H](CC2=N)C(O)=O)c1O
ACDLabs 12.01C(c1c(O)c(C)ncc1COP(O)(O)=O)C2\C(=N)CC(C2)C(O)=O
OpenEye OEToolkits 2.0.6Cc1c(c(c(cn1)COP(=O)(O)O)CC2CC(CC2=N)C(=O)O)O
FormulaC14 H19 N2 O7 P
Name(1S,3S,4E)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid
ChEMBL
DrugBank
ZINC
PDB chain5vwo Chain C Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5vwo Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.
Resolution1.773 Å
Binding residue
(original residue number in PDB)		Y85 G142 V143 F177 W178 G179 R180 E235 D263 I265 Q266 K292
Binding residue
(residue number reindexed from 1)		Y50 G107 V108 F142 W143 G144 R145 E200 D228 I230 Q231 K257
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F177 E230 D263 Q266 K292 T322 R413
Catalytic site (residue number reindexed from 1) F142 E195 D228 Q231 K257 T287 R378
Enzyme Commision number 2.6.1.13: ornithine aminotransferase.
Gene Ontology
Molecular Function
GO:0004587 ornithine aminotransferase activity
GO:0005515 protein binding
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0007601 visual perception
GO:0010121 arginine catabolic process to proline via ornithine
GO:0019544 arginine catabolic process to glutamate
GO:0055129 L-proline biosynthetic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5vwo, PDBe:5vwo, PDBj:5vwo
PDBsum5vwo
PubMed28816437
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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