› 4x7g

X-ray diffraction
1.22Å resolution

Function and Biology Details

Reaction catalysed: 
Precorrin-6B + NADP(+) = precorrin-6A + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Precorrin-6A reductase Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 26.22 KDa
Source organism: Rhodobacter capsulatus SB 1003
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: O68098 (Residues: 1-251; Coverage: 100%)
Gene names: RCAP_rcc02043, cobK
Sequence domains: Precorrin-6x reductase CbiJ/CobK

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
Ligand 3Y8 1 x 3Y8
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 53.09Å b: 60.28Å c: 76.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.197
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

2 review citations

Biosynthesis of the modified tetrapyrroles-the pigments of life.
Bryant et al. (2020)
1 more

1 mention without citation

Crystal structure of CobK reveals strand-swapping between Rossmann-fold domains and molecular basis of the reduced precorrin product trap.
Gu et al. (2015)