› 1gck

X-ray diffraction
2.5Å resolution

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE

Released:
DOI: 10.2210/pdb1gck/pdb
PDB entry 1gck coloured by chain, front view.
PDB entry 1gck coloured by chain, side view.
PDB entry 1gck coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Substrate recognition mechanism of thermophilic dual-substrate enzyme.
Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S
J Biochem 130 89-98 (2001)
PMID: 11432784

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: 385 amino acids
Theoretical weight: 42.13 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56232 (Residues: 1-385; Coverage: 100%)
Gene names: TTHA0046, aspC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 62.75Å b: 74.89Å c: 163.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.205 0.284
Expression system: Escherichia coli

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Citations

2 review citations

Dual substrate recognition of aminotransferases.
Hirotsu et al. (2005)
1 more