› 3q2k

X-ray diffraction
2.13Å resolution

Crystal structure of the WlbA dehydrogenase from Bordetella pertussis in complex with NADH and UDP-GlcNAcA

Released:
DOI: 10.2210/pdb3q2k/pdb
PDB entry 3q2k coloured by chain, front view.
PDB entry 3q2k coloured by chain, side view.
PDB entry 3q2k coloured by chain, top view.
Source organism: Bordetella pertussis Tohama I
Primary publication:
Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid.
Thoden JB, Holden HM
Biochemistry 50 1483-91 (2011)
PMID: 21241053

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable oxidoreductase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 370 amino acids
Theoretical weight: 41.25 KDa
Source organism: Bordetella pertussis Tohama I
Expression system: Escherichia coli
UniProt:
  • Canonical: Q79H45 (Residues: 1-350; Coverage: 100%)
Gene names: BP0093, bplA, wlbA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAI 16 x NAI
Ligand HP7 16 x HP7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 102.261Å b: 319.975Å c: 103.8Å
α: 90° β: 119.07° γ: 90°
R-values:
R R work R free
0.187 0.183 0.269
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
7 other articles

1 mention without citation

Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid.
Thoden et al. (2011)