› 1toe

X-ray diffraction
2Å resolution

Unliganded structure of Hexamutant + A293D mutant of E. coli aspartate aminotransferase

Released:
DOI: 10.2210/pdb1toe/pdb
PDB entry 1toe coloured by chain, front view.
PDB entry 1toe coloured by chain, side view.
PDB entry 1toe 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 Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 43.91 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 SO4 1 x SO4
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2221
Unit cell:
a: 85.713Å b: 152.865Å c: 79.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.202
Expression system: Escherichia coli

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Citations

3 review citations

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