› 2pb0

X-ray diffraction
1.96Å resolution

Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding

Released:
DOI: 10.2210/pdb2pb0/pdb
PDB entry 2pb0 coloured by chain, front view.
PDB entry 2pb0 coloured by chain, side view.
PDB entry 2pb0 coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding.
Rajaram V, Ratna Prasuna P, Savithri HS, Murthy MR
Proteins 70 429-41 (2008)
PMID: 17680699

Function and Biology Details

Reactions catalysed: 
N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154174 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylornithine/succinyldiaminopimelate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 45.47 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P40732 (Residues: 1-405; Coverage: 100%)
Gene names: STM3468, argD, dapC, dtu
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 96.975Å b: 112.053Å c: 65.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.234
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.
Steffen-Munsberg et al. (2015)
2 more

2 mentions without citation

Determination of the structure of the catabolic N-succinylornithine transaminase (AstC) from Escherichia coli.
Newman et al. (2013)
1 more