› 4bif

X-ray diffraction
2.46Å resolution

Biochemical and structural characterisation of a novel manganese- dependent hydroxynitrile lyase from bacteria

Released:
DOI: 10.2210/pdb4bif/pdb
PDB entry 4bif coloured by chain, front view.
PDB entry 4bif coloured by chain, side view.
PDB entry 4bif coloured by chain, top view.
Source organism: Granulicella tundricola MP5ACTX9
Primary publication:
Biochemical and structural characterization of a novel bacterial manganese-dependent hydroxynitrile lyase.
Hajnal I, Lyskowski A, Hanefeld U, Gruber K, Schwab H, Steiner K
FEBS J 280 5815-28 (2013)
PMID: 23981508

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123127 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(R)-mandelonitrile lyase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 156 amino acids
Theoretical weight: 17.37 KDa
Source organism: Granulicella tundricola MP5ACTX9
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E8WYN5 (Residues: 1-131; Coverage: 100%)
Gene name: AciX9_0562
Sequence domains: Cupin domain
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand MN 8 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2221
Unit cell:
a: 126.31Å b: 254.78Å c: 82.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.233
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Enantioselective synthesis of cyanohydrins catalysed by hydroxynitrile lyases - a review.
Bracco et al. (2016)
3 more