Structure of PDB 7lon Chain A

Receptor sequence
>7lonA (length=401) Species: 9606 (Homo sapiens) [Search protein sequence]
PTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSA
VNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVL
PMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISS
STDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAG
VVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDI
VLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSYGGNPLGCRVAIAALE
VLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETKDW
DAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTILS
F
3D structure
PDB7lon Remarkable and Unexpected Mechanism for ( S )-3-Amino-4-(difluoromethylenyl)cyclohex-1-ene-1-carboxylic Acid as a Selective Inactivator of Human Ornithine Aminotransferase.
ChainA
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.13: ornithine aminotransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 7QP A Y55 Y85 G142 V143 F177 W178 E230 D263 I265 Q266 K292 Y18 Y48 G105 V106 F140 W141 E193 D226 I228 Q229 K255
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:7lon, PDBe:7lon, PDBj:7lon
PDBsum7lon
PubMed34014654
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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