X-ray diffraction
1.8Å resolution

E.coli Aspartate aminotransferase-(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP)

Source organism: Escherichia coli K-12
Entry authors: Mascarenhas R, Lehrer H, Liu D, Ringe D

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aspartate aminotransferase Chains: A, D, G, J
Molecule details ›
Chains: A, D, G, J
Length: 396 amino acids
Theoretical weight: 43.62 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • 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 PMP 4 x PMP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P1
Unit cell:
a: 78.897Å b: 84.904Å c: 88.029Å
α: 118.83° β: 90.1° γ: 89.59°
R R work R free
0.164 0.162 0.192
Expression system: Escherichia coli