› 3dqz

X-ray diffraction
2.5Å resolution

Structure of the hydroxynitrile lyase from Arabidopsis thaliana

Released:
DOI: 10.2210/pdb3dqz/pdb
PDB entry 3dqz coloured by chain, front view.
PDB entry 3dqz coloured by chain, side view.
PDB entry 3dqz coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Hydroxynitrile lyases with α/β-hydrolase fold: two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms.
Andexer JN, Staunig N, Eggert T, Kratky C, Pohl M, Gruber K
Chembiochem 13 1932-9 (2012)
PMID: 22851196

Function and Biology Details

Reaction catalysed: 
(R)-mandelonitrile = cyanide + benzaldehyde
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-hydroxynitrile lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 258 amino acids
Theoretical weight: 29.25 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LFT6 (Residues: 1-258; Coverage: 100%)
Gene names: At5g10300, F18D22_70, HNL, MES5
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 50.248Å b: 223.313Å c: 50.201Å
α: 90° β: 101.47° γ: 90°
R-values:
R R work R free
0.159 0.159 0.21
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Immobilisation of hydroxynitrile lyases.
Hanefeld U. (2013)
2 more

5 mentions without citation

Catalytically-active inclusion bodies for biotechnology-general concepts, optimization, and application.
Jäger et al. (2020)
4 more