› 2pzk

X-ray diffraction
2.1Å resolution

Crystal structure of the Bordetella bronchiseptica enzyme WbmG in complex with NAD

Released:
DOI: 10.2210/pdb2pzk/pdb
PDB entry 2pzk coloured by chain, front view.
PDB entry 2pzk coloured by chain, side view.
PDB entry 2pzk coloured by chain, top view.
Source organism: Bordetella bronchiseptica
Primary publication:
Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis.
King JD, Harmer NJ, Preston A, Palmer CM, Rejzek M, Field RA, Blundell TL, Maskell DJ
J Mol Biol 374 749-63 (2007)
PMID: 17950751

Function and Biology Details

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-131524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent epimerase/dehydratase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 35.29 KDa
Source organism: Bordetella bronchiseptica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O87988 (Residues: 1-310; Coverage: 100%)
Gene name: BbLPS1.15
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand NAD 2 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: C2
Unit cell:
a: 192.041Å b: 49.76Å c: 76.023Å
α: 90° β: 101.13° γ: 90°
R-values:
R R work R free
0.188 0.185 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Review: Lipopolysaccharide biosynthesis in Pseudomonas aeruginosa.
King et al. (2009)
1 more

3 mentions without citation

Molecular modeling of the reductase domain to elucidate the reaction mechanism of reduction of peptidyl thioester into its corresponding alcohol in non-ribosomal peptide synthetases.
Manavalan et al. (2010)
2 more