› 1zk2

X-ray diffraction
1.55Å resolution

Orthorhombic crystal structure of the apo-form of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis

Released:
DOI: 10.2210/pdb1zk2/pdb
PDB entry 1zk2 coloured by chain, front view.
PDB entry 1zk2 coloured by chain, side view.
PDB entry 1zk2 coloured by chain, top view.
Source organism: Levilactobacillus brevis
Primary publication:
Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity.
Schlieben NH, Niefind K, Müller J, Riebel B, Hummel W, Schomburg D
J Mol Biol 349 801-13 (2005)
PMID: 15896805

Function and Biology Details

Reaction catalysed: 
An alcohol + NADP(+) = an aldehyde + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183030 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
R-specific alcohol dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 26.71 KDa
Source organism: Levilactobacillus brevis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q84EX5 (Residues: 2-252; Coverage: 100%)
Gene name: radh
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: I222
Unit cell:
a: 55.83Å b: 79.887Å c: 113.112Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.148 0.172
Expression system: Escherichia coli

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Citations

6 review citations

Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family.
Stuermer et al. (2007)
5 more

1 mention without citation

Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways.
Hermann et al. (2018)