› 1iug

X-ray diffraction
2.2Å resolution

The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus

Released:
DOI: 10.2210/pdb1iug/pdb
PDB entry 1iug coloured by chain, front view.
PDB entry 1iug coloured by chain, side view.
PDB entry 1iug coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV.
Katsura Y, Shirouzu M, Yamaguchi H, Ishitani R, Nureki O, Kuramitsu S, Hayashi H, Yokoyama S
Proteins 55 487-92 (2004)
PMID: 15103612

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class V domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 352 amino acids
Theoretical weight: 38.26 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P83786 (Residues: 1-352; Coverage: 100%)
Sequence domains: Aminotransferase class-V
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: RIGAKU, SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 92.849Å b: 135.33Å c: 133.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.236
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Enzymatic strategies for asymmetric synthesis.
Hall M. (2021)
4 other articles

1 mention without citation

Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.
Fleischman et al. (2014)