3aat

X-ray diffraction
2.8Å resolution

ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE

Released:

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: 43.61 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: 156Å b: 87.6Å c: 78.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 not available not available
Expression system: Escherichia coli