› 2g4l

X-ray diffraction
1.84Å resolution

Function and Biology Details

Reaction catalysed: 
An aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156604 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(S)-hydroxynitrile lyase Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 29.34 KDa
Source organism: Hevea brasiliensis
UniProt:
  • Canonical: P52704 (Residues: 1-257; Coverage: 100%)
Gene name: HNL
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand CL 1 x CL
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: C2221
Unit cell:
a: 47.09Å b: 106.05Å c: 128.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.197

Quick links

Citations

5 review citations

Conformational selection in trypsin-like proteases.
Pozzi et al. (2012)
4 more

1 mention without citation

Designing Efficient Enzymes: Eight Predicted Mutations Convert a Hydroxynitrile Lyase into an Efficient Esterase.
Casadevall et al. (2023)