› 5e46

X-ray diffraction
1.85Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxynitrile lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.54 KDa
Source organism: Davallia tyermanii
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1C9V3S9 (Residues: 1-184; Coverage: 100%)
Gene name: HNL1
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 73.633Å b: 94.02Å c: 117.054Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.155 0.192
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Progress in Stereoselective Construction of C-C Bonds Enabled by Aldolases and Hydroxynitrile Lyases.
Liu et al. (2021)
9 other articles

1 mention without citation

Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily.
Lanfranchi et al. (2017)