› 4e5k

X-ray diffraction
1.95Å resolution

Thermostable phosphite dehydrogenase in complex with NAD and sulfite

Released:
DOI: 10.2210/pdb4e5k/pdb
PDB entry 4e5k coloured by chain, front view.
PDB entry 4e5k coloured by chain, side view.
PDB entry 4e5k coloured by chain, top view.
Source organism: Pseudomonas stutzeri
Primary publication:
Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration.
Zou Y, Zhang H, Brunzelle JS, Johannes TW, Woodyer R, Hung JE, Nair N, van der Donk WA, Zhao H, Nair SK
Biochemistry 51 4263-70 (2012)
PMID: 22564171

Function and Biology Details

Reaction catalysed: 
Phosphonate + NAD(+) + H(2)O = phosphate + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130641 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphonate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 329 amino acids
Theoretical weight: 35.91 KDa
Source organism: Pseudomonas stutzeri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69054 (Residues: 1-329; Coverage: 98%)
Gene name: ptxD
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand SO3 4 x SO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 73.06Å b: 114.18Å c: 88.31Å
α: 90° β: 112.33° γ: 90°
R-values:
R R work R free
0.221 0.219 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Engineering redox balance through cofactor systems.
Chen et al. (2014)
1 more

6 mentions without citation

A Hitchhiker's Guide to Supplying Enzymatic Reducing Power into Synthetic Cells.
Partipilo et al. (2023)
5 more