› 1e8d

X-ray diffraction
2.2Å resolution

MECHANISTIC ASPECTS OF CYANOGENESIS FROM ACTIVE SITE MUTANT SER80ALA OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH ACETONE CYANOHYDRIN

Released:
DOI: 10.2210/pdb1e8d/pdb
PDB entry 1e8d coloured by chain, front view.
PDB entry 1e8d coloured by chain, side view.
PDB entry 1e8d coloured by chain, top view.
Source organism: Manihot esculenta
Primary publication:
Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin.
Lauble H, Miehlich B, Förster S, Wajant H, Effenberger F
Protein Sci 10 1015-22 (2001)
PMID: 11316882

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(S)-hydroxynitrile lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 29.82 KDa
Source organism: Manihot esculenta
Expression system: Escherichia coli
UniProt:
  • Canonical: P52705 (Residues: 2-258; Coverage: 100%)
Gene name: HNL
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CNH 4 x CNH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P41212
Unit cell:
a: 105.9Å b: 105.9Å c: 187.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.238
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The BioCassava plus program: biofortification of cassava for sub-Saharan Africa.
Sayre et al. (2011)
2 more

3 mentions without citation

Catalytic Promiscuity of Ancestral Esterases and Hydroxynitrile Lyases.
Devamani et al. (2016)
2 more