› 2e54

X-ray diffraction
1.5Å resolution

Crystal structure of acetylornithine aminotransferase from Thermotoga maritima

Released:
DOI: 10.2210/pdb2e54/pdb
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PDB entry 2e54 coloured by chain, front view.
PDB entry 2e54 coloured by chain, side view.
PDB entry 2e54 coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Entry authors: Mizutani H, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed: 
N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + 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-194886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylornithine aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 385 amino acids
Theoretical weight: 42.94 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X2A5 (Residues: 1-385; Coverage: 100%)
Gene names: TM_1785, argD
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
2 bound ligands:
Ligand NA 2 x NA
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21212
Unit cell:
a: 67.222Å b: 115.697Å c: 52.448Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.213
Expression system: Escherichia coli

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