› 3o9z

X-ray diffraction
1.45Å resolution

Crystal structure of the WlbA (WbpB) dehydrogenase from Thermus thermophilus in complex with NAD and alpha-ketoglutarate at 1.45 angstrom resolution

Released:
DOI: 10.2210/pdb3o9z/pdb
PDB entry 3o9z coloured by chain, front view.
PDB entry 3o9z coloured by chain, side view.
PDB entry 3o9z coloured by chain, top view.
Source organism: Thermus thermophilus HB27
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

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180881 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipopolysaccaride biosynthesis protein wbpB Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 312 amino acids
Theoretical weight: 34.83 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q72KX8 (Residues: 1-310; Coverage: 100%)
Gene names: TT_C0287, wbpB
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand NAD 4 x NAD
Ligand AKG 4 x AKG
Ligand CL 4 x CL
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 71.781Å b: 68.199Å c: 164.053Å
α: 90° β: 94.66° γ: 90°
R-values:
R R work R free
0.195 0.194 0.226
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.
Ren et al. (2022)
9 other articles

2 mentions without citation

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