› 3oa2

X-ray diffraction
1.5Å resolution

Crystal structure of the WlbA (WbpB) dehydrogenase from Pseudomonas aeruginosa in complex with NAD at 1.5 angstrom resolution

Released:
DOI: 10.2210/pdb3oa2/pdb
PDB entry 3oa2 coloured by chain, front view.
PDB entry 3oa2 coloured by chain, side view.
PDB entry 3oa2 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid .
Thoden JB, Holden HM
Biochemistry 49 7939-48 (2010)
PMID: 20690587

Function and Biology Details

Reaction catalysed: 
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD(+) = UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124393 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 318 amino acids
Theoretical weight: 35.99 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G3XD23 (Residues: 1-316; Coverage: 100%)
Gene names: PA3158, wbpB, wlbA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 73.215Å b: 129.562Å c: 145.237Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases.
Taberman et al. (2016)
1 more

1 mention without citation

Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid .
Thoden et al. (2010)