1asb

X-ray diffraction
2.6Å resolution

THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE

Released:
Source organism: Escherichia coli
Entry authors: Schumacher C, Ringe D

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 43.58 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 159.12Å b: 86.15Å c: 79.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 not available
Expression system: Escherichia coli