› 1ahx

X-ray diffraction
2Å resolution

ASPARTATE AMINOTRANSFERASE HEXAMUTANT

Released:
DOI: 10.2210/pdb1ahx/pdb
PDB entry 1ahx coloured by chain, front view.
PDB entry 1ahx coloured by chain, side view.
PDB entry 1ahx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN
Nat Struct Biol 2 548-53 (1995)
PMID: 7664122

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
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-132575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 43.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00509 (Residues: 1-396; Coverage: 100%)
Gene names: JW0911, aspC, b0928
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 84.98Å b: 78.69Å c: 89.28Å
α: 90° β: 118.32° γ: 90°
R-values:
R R work R free
0.226 not available not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
5 more

2 mentions without citation

Structural Basis for the Inhibition of Voltage-gated Sodium Channels by Conotoxin μO§-GVIIJ.
Green et al. (2016)
1 more