X-ray diffraction
1.62Å resolution

Actinobacterial 2-hydroxyacyl-CoA lyase (AcHACL) mutant E493A structure in complex with substrate 2-HIB-CoA and inactive cofactor 3-deaza-ThDP


Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
2-hydroxyacyl-CoA lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 612 amino acids
Theoretical weight: 65.3 KDa
Source organism: Actinomycetospora chiangmaiensis DSM 45062
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P0DUV9 (Residues: 1-590; Coverage: 100%)

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 103.915Å b: 146.718Å c: 174.413Å
α: 90° β: 90° γ: 90°
R R work R free
0.155 0.154 0.186
Expression system: Escherichia coli BL21(DE3)