› 1ahf

X-ray diffraction
2.3Å resolution

ASPARTATE AMINOTRANSFERASE HEXAMUTANT

Released:
DOI: 10.2210/pdb1ahf/pdb
PDB entry 1ahf coloured by chain, front view.
PDB entry 1ahf coloured by chain, side view.
PDB entry 1ahf 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
2 bound ligands:
Ligand IOP 1 x IOP
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 85.92Å b: 79.39Å c: 88.8Å
α: 90° β: 118.99° γ: 90°
R-values:
R R work R free
0.232 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