X-ray diffraction
2.1Å resolution

Aspartate Aminotransferase from Phormidium lapideum

Source organism: Phormidium lapideum
Entry authors: Kim H, Sawa Y, Hamada K

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 42.14 KDa
Source organism: Phormidium lapideum
Expression system: Escherichia coli
  • Canonical: Q8RR70 (Residues: 1-388; Coverage: 100%)
Gene name: aspC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL24XU
Spacegroup: C2221
Unit cell:
a: 120.22Å b: 131.26Å c: 107.85Å
α: 90° β: 90° γ: 90°
R R work R free
0.198 0.198 0.238
Expression system: Escherichia coli