Structure of PDB 4jev Chain A Binding Site BS01

Receptor Information
>4jev Chain A (length=401) 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]
AITRATFDEVILPVYAPADFIPVKGKGSRVWDQQGKEYIDFAGGIAVTAL
GHCHPALVEALKSQGETLWHTSNVFTNEPALRLGRKLIDATFAERVLFMN
SGTEANETAFKLARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPK
YSDGFGPKPADIIHVPFNDLHAVKAVMDDHTCAVVVEPIQGEGGVQAATP
EFLKGLRDLCDEHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKA
LGGGFPVSAMLTTQEIASAFHVGSHGSTYGGNPLACAVAGATFDIINTPE
VLQGIHTKRQQFVQHLQAIDEQFDIFSDIRGMGLLIGAELKPKYKGRARD
FLYAGAEAGVMVLNAGADVMRFAPSLVVEEADIHEGMQRFAQAVGKVVAL
E
Ligand information
Ligand IDPXG
InChIInChI=1S/C15H17N2O7P/c1-9-14(18)13(11(6-16-9)8-24-25(21,22)23)7-17-12-4-2-3-10(5-12)15(19)20/h2-6,17-18H,7-8H2,1H3,(H,19,20)(H2,21,22,23)
InChIKeyWSOQXCGRIUHULI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)c1cc(ccc1)NCc2c(cnc(c2O)C)COP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cccc(c2)C(=O)O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CNc2cccc(c2)C(O)=O)c1O
FormulaC15 H17 N2 O7 P
Name3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID
ChEMBL
DrugBank
ZINC
PDB chain4jev Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4jev Conformational transitions, ligand specificity and catalysis in N-acetylornithine aminotransferase: Implications on drug designing and rational enzyme engineering in omega aminotransferases.
Resolution1.67 Å
Binding residue
(original residue number in PDB)		I51 S107 G108 T109 F141 H142 E193 E198 D226 V228 Q229 K255 R377
Binding residue
(residue number reindexed from 1)		I45 S101 G102 T103 F135 H136 E187 E192 D220 V222 Q223 K249 R371
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) F135 E187 D220 Q223 K249 T278 R371
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:4jev, PDBe:4jev, PDBj:4jev
PDBsum4jev
PubMed
UniProtP40732|ARGD_SALTY Acetylornithine/succinyldiaminopimelate aminotransferase (Gene Name=argD)

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