› 1gxs

X-ray diffraction
2.3Å resolution

Crystal Structure of Hydroxynitrile Lyase from Sorghum bicolor in Complex with Inhibitor Benzoic Acid: a novel cyanogenic enzyme

Released:
DOI: 10.2210/pdb1gxs/pdb
PDB entry 1gxs coloured by chain, front view.
PDB entry 1gxs coloured by chain, side view.
PDB entry 1gxs coloured by chain, top view.
Source organism: Sorghum bicolor
Primary publication:
Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme.
Lauble H, Miehlich B, Förster S, Wajant H, Effenberger F
Biochemistry 41 12043-50 (2002)
PMID: 12356304

Function and Biology Details

Reaction catalysed: 
(S)-4-hydroxymandelonitrile = cyanide + 4-hydroxybenzaldehyde
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156607 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
P-(S)-hydroxymandelonitrile lyase chain A Chains: A, C
Molecule details ›
Chains: A, C
Length: 270 amino acids
Theoretical weight: 30.4 KDa
Source organism: Sorghum bicolor
UniProt:
  • Canonical: P52708 (Residues: 56-325; Coverage: 57%)
Sequence domains: Serine carboxypeptidase
Structure domains: alpha/beta hydrolase
P-(S)-hydroxymandelonitrile lyase chain B Chains: B, D
Molecule details ›
Chains: B, D
Length: 158 amino acids
Theoretical weight: 17.71 KDa
Source organism: Sorghum bicolor
UniProt:
  • Canonical: P52708 (Residues: 338-495; Coverage: 33%)
Sequence domains: Serine carboxypeptidase
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
3 bound ligands:
Ligand BEZ 2 x BEZ
Ligand DKA 2 x DKA
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 150.7Å b: 103.7Å c: 90.6Å
α: 90° β: 101.3° γ: 90°
R-values:
R R work R free
0.165 0.165 0.222

Quick links

Citations

5 review citations

Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry.
Purkarthofer et al. (2007)
4 more

5 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
4 more