Structure of PDB 4jez Chain A Binding Site BS01

Receptor Information
>4jez Chain A (length=378) 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]
ADFIPVKGKGSRVWDQQGKEYIDFAGGIAVTALGHCHPALVEALKSQGET
LWHTSRVFTNEPALRLGRKLIDATFAERVLFMNSGTEANETAFKLARHYA
CVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPADIIHVPF
NDLHAVKAVMDDHTCAVVVEPIQGEGGVQAATPEFLKGLRDLCDEHQALL
VFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPVSAMLTTQEIA
SAFGSTYGGNPLACAVAGATFDIINTPEVLQGIHTKRQQFVQHLQAIDEQ
FDIFSDIRGMGLLIGAELKPKYKGRARDFLYAGAEAGVMVLNAGADVMRF
APSLVVEEADIHEGMQRFAQAVGKVVAL
Ligand information
Ligand IDP00
InChIInChI=1S/C12H18N3O8P/c1-7-11(16)9(5-15-22-3-2-10(13)12(17)18)8(4-14-7)6-23-24(19,20)21/h4-5,10,16H,2-3,6,13H2,1H3,(H,17,18)(H2,19,20,21)/b15-5+/t10-/m0/s1
InChIKeyHDUKWWSNPJPYAB-XSFFOXFNSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Cc1ncc(CO[P](O)(O)=O)c(C=NOCC[CH](N)C(O)=O)c1O
OpenEye OEToolkits 1.7.6Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/OCC[C@@H](C(=O)O)N)O
OpenEye OEToolkits 1.7.6Cc1c(c(c(cn1)COP(=O)(O)O)C=NOCCC(C(=O)O)N)O
CACTVS 3.370Cc1ncc(CO[P](O)(O)=O)c(\C=N\OCC[C@H](N)C(O)=O)c1O
FormulaC12 H18 N3 O8 P
Name(2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid
ChEMBL
DrugBank
ZINCZINC000098209278
PDB chain4jez Chain A Residue 511 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4jez 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)		I51 G108 T109 N112 F141 H142 E193 E198 D226 V228 K255
Binding residue
(residue number reindexed from 1)		I28 G85 T86 N89 F118 H119 E170 E175 D203 V205 K232
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) F118 E170 D203 Q206 K232 T256 R349
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:4jez, PDBe:4jez, PDBj:4jez
PDBsum4jez
PubMed
UniProtP40732|ARGD_SALTY Acetylornithine/succinyldiaminopimelate aminotransferase (Gene Name=argD)

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