› 1czc

X-ray diffraction
2.5Å resolution

ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH GLUTARIC ACID

Released:
DOI: 10.2210/pdb1czc/pdb
PDB entry 1czc coloured by chain, front view.
PDB entry 1czc coloured by chain, side view.
PDB entry 1czc coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex.
Oue S, Okamoto A, Yano T, Kagamiyama H
J Biochem 127 337-43 (2000)
PMID: 10731702

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: 43.66 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 GUA 1 x GUA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 156.35Å b: 85.02Å c: 78.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.182 0.243
Expression system: Escherichia coli

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Citations

1 review citation

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
2 other articles