Structure of PDB 2byj Chain A Binding Site BS01
Receptor Information
>2byj Chain A (length=404) Species:
9606
(Homo sapiens) [
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GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSI
SAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHK
VLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAI
SSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE
AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRP
DIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIA
ALEVLEEENLAENADKLGIILRNELMKLPSDVVTAVRGKGLLNAIVIKET
KDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT
ILSF
Ligand information
Ligand ID
PLP
InChI
InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKey
NGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0
Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04
O=P(O)(O)OCc1cnc(c(O)c1C=O)C
Formula
C8 H10 N O6 P
Name
PYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBL
CHEMBL82202
DrugBank
DB00114
ZINC
ZINC000001532514
PDB chain
2byj Chain A Residue 500 [
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Receptor-Ligand Complex Structure
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PDB
2byj
Determinants of Substrate Specificity in Omega-Aminotransferases.
Resolution
3.02 Å
Binding residue
(original residue number in PDB)
G142 V143 F177 W178 D263 I265 Q266 K292
Binding residue
(residue number reindexed from 1)
G107 V108 F142 W143 D228 I230 Q231 K257
Annotation score
1
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.
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2byj
,
PDBe:2byj
,
PDBj:2byj
PDBsum
2byj
PubMed
16096275
UniProt
P04181
|OAT_HUMAN Ornithine aminotransferase, mitochondrial (Gene Name=OAT)
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