› 1ix7

X-ray diffraction
2.2Å resolution

Aspartate Aminotransferase Active Site Mutant V39F maleate complex

Released:
DOI: 10.2210/pdb1ix7/pdb
PDB entry 1ix7 coloured by chain, front view.
PDB entry 1ix7 coloured by chain, side view.
PDB entry 1ix7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.
Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H
J Biol Chem 278 9481-8 (2003)
PMID: 12488449

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 Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 43.67 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 1 x PLP
1 bound ligand:
Ligand MAE 1 x MAE
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 158.445Å b: 85.833Å c: 79.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.247
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Features and technical applications of ω-transaminases.
Malik et al. (2012)
1 more