Structure of PDB 7ta0 Chain A

Receptor sequence
>7ta0A (length=403) Species: 9606 (Homo sapiens) [Search protein sequence]
PPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYS
AVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKV
LPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAIS
SSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEA
GVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPD
IVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAA
LEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKETK
DWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKTI
LSF
3D structure
PDB7ta0 Determination of the pH dependence, substrate specificity, and turnovers of alternative substrates for human ornithine aminotransferase.
ChainA
Resolution2.33 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 I3B A Y55 Y85 G142 V143 F177 W178 D263 I265 Q266 K292 Y19 Y49 G106 V107 F141 W142 D227 I229 Q230 K256
BS02 I3B A S321 T322 S285 T286
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:7ta0, PDBe:7ta0, PDBj:7ta0
PDBsum7ta0
PubMed35460691
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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