Structure of PDB 7jx9 Chain A Binding Site BS01

Receptor Information
>7jx9 Chain A (length=402) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSA
VNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVL
PMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISS
STDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAG
VVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDI
VLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAAL
EVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETKD
WDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTIL
SF
Ligand information
Ligand IDIF1
InChIInChI=1S/C17H18F5N2O7P/c1-7-14(25)11(9(4-23-7)6-31-32(28,29)30)5-24-12-3-8(16(26)27)2-10(12)13(15(18)19)17(20,21)22/h4-5,8,10,12,25H,2-3,6H2,1H3,(H,26,27)(H2,28,29,30)/b24-5+/t8-,10+,12-/m0/s1
InChIKeyNXIZEOJYEPCEAL-UJKLFKHKSA-N
SMILES
SoftwareSMILES
CACTVS 3.385Cc1ncc(CO[P](O)(O)=O)c(C=N[CH]2C[CH](C[CH]2C(=C(F)F)C(F)(F)F)C(O)=O)c1O
ACDLabs 12.01C(C2CC(N=[C@H]c1c(c(ncc1COP(=O)(O)O)C)O)C(C2)C(/C(F)(F)F)=C(/F)F)(O)=O
OpenEye OEToolkits 2.0.7Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/C2C[C@H](C[C@H]2C(=C(F)F)C(F)(F)F)C(=O)O)O
CACTVS 3.385Cc1ncc(CO[P](O)(O)=O)c(C=N[C@H]2C[C@H](C[C@H]2C(=C(F)F)C(F)(F)F)C(O)=O)c1O
OpenEye OEToolkits 2.0.7Cc1c(c(c(cn1)COP(=O)(O)O)C=NC2CC(CC2C(=C(F)F)C(F)(F)F)C(=O)O)O
FormulaC17 H18 F5 N2 O7 P
Name(1S,3S,4S)-3-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-(1,1,3,3,3-pentafluoroprop-1-en-2-yl)cyclopentane-1-carboxylic acid
ChEMBL
DrugBank
ZINC
PDB chain7jx9 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7jx9 Structural and Kinetic Analyses Reveal the Dual Inhibition Modes of Ornithine Aminotransferase by (1 S ,3 S )-3-Amino-4-(hexafluoropropan-2-ylidenyl)-cyclopentane-1-carboxylic Acid (BCF 3 ).
Resolution1.96 Å
Binding residue
(original residue number in PDB)		Y55 Y85 G142 V143 F177 W178 E235 D263 I265 Q266 K292 R413
Binding residue
(residue number reindexed from 1)		Y18 Y48 G105 V106 F140 W141 E198 D226 I228 Q229 K255 R376
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) F140 E193 D226 Q229 K255 T285 R376
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:7jx9, PDBe:7jx9, PDBj:7jx9
PDBsum7jx9
PubMed33316155
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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