› 1g4x

X-ray diffraction
2.2Å resolution

ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/R292L

Released:
DOI: 10.2210/pdb1g4x/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1g4x coloured by chain, front view.
PDB entry 1g4x coloured by chain, side view.
PDB entry 1g4x coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
Mizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H
Biochemistry 40 353-60 (2001)
PMID: 11148029

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: 43.53 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
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 155.04Å b: 88.75Å c: 80.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 not available not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Aspartate aminotransferase: an old dog teaches new tricks.
Toney MD. (2014)
2 more

1 mention without citation

Discriminative structural approaches for enzyme active-site prediction.
Kato et al. (2011)