› 2ord

X-ray diffraction
1.4Å resolution

Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution

Released:
DOI: 10.2210/pdb2ord/pdb
PDB entry 2ord coloured by chain, front view.
PDB entry 2ord coloured by chain, side view.
PDB entry 2ord coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 397 amino acids
Theoretical weight: 44.87 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 2 x PLP
1 bound ligand:
Ligand GOL 17 x GOL
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 90.948Å b: 95.628Å c: 96.089Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.148 0.17
Expression system: Escherichia coli

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