› 1ari

X-ray diffraction
2.3Å resolution

Aspartate aminotransferase, W140H mutant, maleate complex

Released:
DOI: 10.2210/pdb1ari/pdb
PDB entry 1ari coloured by chain, front view.
PDB entry 1ari coloured by chain, side view.
PDB entry 1ari coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.
Vacca RA, Christen P, Malashkevich VN, Jansonius JN, Sandmeier E
Eur J Biochem 227 481-7 (1995)
PMID: 7851426

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: 43.57 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 MAE 2 x MAE
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 86.4Å b: 79Å c: 90.8Å
α: 90° β: 118.8° γ: 90°
R-values:
R R work R free
0.21 not available not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

D-Aspartate acts as a signaling molecule in nervous and neuroendocrine systems.
Ota et al. (2012)
12 other articles

3 mentions without citation

A functional-phylogenetic classification system for transmembrane solute transporters.
Saier MH. (2000)
2 more