› 1bjw

X-ray diffraction
1.8Å resolution

ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS

Released:
DOI: 10.2210/pdb1bjw/pdb
PDB entry 1bjw coloured by chain, front view.
PDB entry 1bjw coloured by chain, side view.
PDB entry 1bjw coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K
Biochemistry 38 2413-24 (1999)
PMID: 10029535

Function and Biology Details

Reactions catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-arogenate + oxaloacetate = prephenate + L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176335 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate/prephenate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 42.05 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56232 (Residues: 1-382; Coverage: 99%)
Gene names: TTHA0046, aspC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 61.6Å b: 113.86Å c: 124.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.269
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
4 more

5 mentions without citation

Protein subunit interfaces: heterodimers versus homodimers.
Zhanhua et al. (2005)
4 more