Structure of PDB 4jey Chain B Binding Site BS01

Receptor Information
>4jey Chain B (length=388) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPVYAPADFIPVKGKGSRVWDQQGKEYIDFAGGIAVTALGHCHPALVEAL
KSQGETLWHTSNVFTNEPALRLGRKLIDATFAERVLFMNSGTEANETAFK
LARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPAD
IIHVPFNDLHAVKAVMDDHTCAVVVEPIQGAGGVQAATPEFLKGLRDLCD
EHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPVSAML
TTQEIASAFHVGSHGSTYGGNPLACAVAGATFDIINTPEVLQGIHTKRQQ
FVQHLQAIDEQFDIFSDIRGMGLLIGAELKPKYKGRARDFLYAGAEAGVM
VLNAGADVMRFAPSLVVEEADIHEGMQRFAQAVGKVVA
Ligand information
Ligand IDPLP
InChIInChI=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)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain4jey Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4jey Conformational transitions, ligand specificity and catalysis in N-acetylornithine aminotransferase: Implications on drug designing and rational enzyme engineering in omega aminotransferases
Resolution1.55 Å
Binding residue
(original residue number in PDB)		G108 T109 F141 H142 E193 D226 V228 Q229 K255
Binding residue
(residue number reindexed from 1)		G91 T92 F124 H125 E176 D209 V211 Q212 K238
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F141 E193 D226 Q229 K255 T284 R377
Catalytic site (residue number reindexed from 1) F124 E176 D209 Q212 K238 T267 R360
Enzyme Commision number 2.6.1.11: acetylornithine transaminase.
2.6.1.17: succinyldiaminopimelate transaminase.
Gene Ontology
Molecular Function
GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
GO:0008483 transaminase activity
GO:0009016 succinyldiaminopimelate transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006525 arginine metabolic process
GO:0006526 L-arginine biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4jey, PDBe:4jey, PDBj:4jey
PDBsum4jey
PubMed
UniProtP40732|ARGD_SALTY Acetylornithine/succinyldiaminopimelate aminotransferase (Gene Name=argD)

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