Structure of PDB 4adb Chain B Binding Site BS01

Receptor Information
>4adb Chain B (length=401) Species: 511693 (Escherichia coli BL21) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNA
LGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFC
NSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQP
AYSQDFAPLPADIRHAAYNDINSASALIDDSTCAVIVEPIQGEGGVVPAS
NAFLQGLRELCNRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAK
ALGGGFPVGALLATEECARVMTVGTHGTTYGGNPLASAVAGKVLELINTP
EMLNGVKQRHDWFVERLNTINHRYGLFSEVRGLGLLIGCVLNADYAGQAK
QISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVS
R
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 chain4adb Chain B Residue 1404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4adb Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (Astc) from Escherichia Coli.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		S104 G105 A106 F138 H139 D223 V225 Q226 K252
Binding residue
(residue number reindexed from 1)		S102 G103 A104 F136 H137 D221 V223 Q224 K250
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F138 E190 D223 Q226 K252 T281 R374
Catalytic site (residue number reindexed from 1) F136 E188 D221 Q224 K250 T279 R372
Enzyme Commision number 2.6.1.81: succinylornithine transaminase.
Gene Ontology
Molecular Function
GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0043825 succinylornithine transaminase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006525 arginine metabolic process
GO:0006526 L-arginine biosynthetic process
GO:0006527 arginine catabolic process
GO:0006593 ornithine catabolic process
GO:0019544 arginine catabolic process to glutamate
GO:0019545 arginine catabolic process to succinate
GO:0042450 arginine biosynthetic process via ornithine

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4adb, PDBe:4adb, PDBj:4adb
PDBsum4adb
PubMed23484010
UniProtP77581|ASTC_ECOLI Succinylornithine transaminase (Gene Name=astC)

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