› 5eaa

X-ray diffraction
2.4Å resolution

ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION

Released:
DOI: 10.2210/pdb5eaa/pdb
PDB entry 5eaa coloured by chain, front view.
PDB entry 5eaa coloured by chain, side view.
PDB entry 5eaa coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
Jeffery CJ, Gloss LM, Petsko GA, Ringe D
Protein Eng 13 105-12 (2000)
PMID: 10708649

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: 43.6 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

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 156.27Å b: 86.94Å c: 79.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 not available
Expression system: Escherichia coli

Quick links

Citations

18 citation in other articles

Identification of specific interactions that drive ligand-induced closure in five enzymes with classic domain movements.
Hayward S. (2004)
17 more

1 mention without citation

Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction.
Smith et al. (2008)