Structure of PDB 2pb0 Chain A Binding Site BS01

Receptor Information
>2pb0 Chain A (length=389) 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]
TFDEVILPVYAPADFIPVKGKGSRVWDQQGKEYIDFAGGIAVTALGHCHP
ALVEALKSQGETLWHTSNVFTNEPALRLGRKLIDATFAERVLFMNSGTEA
NETAFKLARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGF
GPKPADIIHVPFNDLHAVKAVMDDHTCAVVVEPIQGEGGVQAATPEFLKG
LRDLCDEHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGF
PVSAMLTTQEIASAFGSTYGGNPLACAVAGAAFDIINTPEVLQGIHTKRQ
QFVQHLQAIDEQFDIFSDIRGMGLLIGAELKPKYKGRARDFLYAGAEAGV
MVLNAGADVMRFAPSLVVEEADIHEGMQRFAQAVGKVVA
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 chain2pb0 Chain A Residue 555 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2pb0 Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: Studies on substrate specificity and inhibitor binding
Resolution1.96 Å
Binding residue
(original residue number in PDB)		S107 G108 T109 F141 H142 E193 D226 V228 Q229 K255
Binding residue
(residue number reindexed from 1)		S96 G97 T98 F130 H131 E182 D215 V217 Q218 K244
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) F130 E182 D215 Q218 K244 T268 R361
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:2pb0, PDBe:2pb0, PDBj:2pb0
PDBsum2pb0
PubMed17680699
UniProtP40732|ARGD_SALTY Acetylornithine/succinyldiaminopimelate aminotransferase (Gene Name=argD)

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