› 1tok

X-ray diffraction
1.85Å resolution

Maleic acid-bound structure of SRHEPT mutant of E. coli aspartate aminotransferase

Released:
DOI: 10.2210/pdb1tok/pdb
PDB entry 1tok coloured by chain, front view.
PDB entry 1tok coloured by chain, side view.
PDB entry 1tok coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase.
Chow MA, McElroy KE, Corbett KD, Berger JM, Kirsch JF
Biochemistry 43 12780-7 (2004)
PMID: 15461450

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: 43.83 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

1 bound ligand:
Ligand MAE 2 x MAE
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P63
Unit cell:
a: 140.142Å b: 140.142Å c: 81.075Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.227
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
2 more

2 mentions without citation

CSAR benchmark exercise of 2010: combined evaluation across all submitted scoring functions.
Smith et al. (2011)
1 more