› 5l1n

X-ray diffraction
3.6Å resolution

Pyrococcus horikoshii CoA Disulfide Reductase Quadruple Mutant

Released:
DOI: 10.2210/pdb5l1n/pdb
PDB entry 5l1n coloured by chain, front view.
PDB entry 5l1n coloured by chain, side view.
PDB entry 5l1n coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry.
Sea K, Lee J, To D, Chen B, Sazinsky MH, Crane EJ
FEBS Open Bio 8 1083-1092 (2018)
PMID: 29988575

Function and Biology Details

Reaction catalysed: 
2 CoA + NADP(+) = CoA-disulfide + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H coenzyme A polysulfide/persulfide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 453 amino acids
Theoretical weight: 49.82 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: O58308 (Residues: 1-445; Coverage: 100%)
Gene name: PH0572
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand COA 2 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: R3
Unit cell:
a: 191.965Å b: 191.965Å c: 74.866Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.245 0.29
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

2 citation in other articles

Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH-binding properties.
Shoor et al. (2021)
1 more

1 mention without citation

A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry.
Sea et al. (2018)