› 1asg

X-ray diffraction
2.8Å resolution

THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE

Released:
DOI: 10.2210/pdb1asg/pdb
PDB entry 1asg coloured by chain, front view.
PDB entry 1asg coloured by chain, side view.
PDB entry 1asg coloured by chain, top view.
Source organism: Escherichia coli
Entry authors: Schumacher C, Ringe D

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
1 bound ligand:
Ligand MAE 1 x MAE
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 157.8Å b: 85.5Å c: 78.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 not available
Expression system: Escherichia coli

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