X-ray diffraction
1.8Å resolution

Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from Sulfolobus solfataricus


Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aminotransferase class V domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 384 amino acids
Theoretical weight: 42.03 KDa
Source organism: Saccharolobus solfataricus P2
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q97VM5 (Residues: 1-384; Coverage: 100%)
Gene names: SSO2597, agxT
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments

Cofactor: Ligand PMP 2 x PMP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2
Unit cell:
a: 160.13Å b: 55.05Å c: 101.59Å
α: 90° β: 111.03° γ: 90°
R R work R free
0.191 0.189 0.234
Expression system: Escherichia coli BL21(DE3)