Structure of PDB 8ez1 Chain A

Receptor sequence
>8ez1A (length=402) Species: 9606 (Homo sapiens) [Search protein sequence]
PTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSA
VNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVL
PMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISS
STDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAG
VVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDI
VLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAAL
EVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETKD
WDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTIL
SF
3D structure
PDB8ez1 Structural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3 S ,4 S )-3-Amino-4-fluorocyclopentenecarboxylic Acid.
ChainA
Resolution1.91 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 X8B A Y85 G142 V143 F177 W178 E235 D263 I265 Q266 K292 R413 Y48 G105 V106 F140 W141 E198 D226 I228 Q229 K255 R376
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:8ez1, PDBe:8ez1, PDBj:8ez1
PDBsum8ez1
PubMed36770800
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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