Structure of PDB 2byj Chain A

Receptor sequence
>2byjA (length=404) Species: 9606 (Homo sapiens) [Search protein sequence]
GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSI
SAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHK
VLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAI
SSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE
AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRP
DIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIA
ALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKET
KDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT
ILSF
3D structure
PDB2byj Determinants of Substrate Specificity in Omega-Aminotransferases.
ChainA
Resolution3.02 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 PLP A G142 V143 F177 W178 D263 I265 Q266 K292 G107 V108 F142 W143 D228 I230 Q231 K257
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:2byj, PDBe:2byj, PDBj:2byj
PDBsum2byj
PubMed16096275
UniProtP04181|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)

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