› 6m2a

X-ray diffraction
2.23Å resolution

A non-His-rich type of chimeric sirohydrochlorin nickelochelatase CfbA from M. jannaschii and M. barkeri

Released:
DOI: 10.2210/pdb6m2a/pdb
PDB entry 6m2a coloured by chain, front view.
PDB entry 6m2a coloured by chain, side view.
PDB entry 6m2a coloured by chain, top view.
Source organisms:
Primary publication:
The nickel-sirohydrochlorin formation mechanism of the ancestral class II chelatase CfbA in coenzyme F430 biosynthesis.
Fujishiro T, Ogawa S
OpenAccess logo Chem Sci 12 2172-2180 (2021)
PMID: 34163982

Function and Biology Details

Reactions catalysed: 
Ni-sirohydrochlorin + 2 H(+) = sirohydrochlorin + Ni(2+)
Cobalt-precorrin-2 + 2 H(+) = precorrin-2 + Co(2+)
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-158388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sirohydrochlorin cobaltochelatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.02 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q58380 (Residues: 1-86, 119-143; Coverage: 78%)
  • Canonical: P61816 (Residues: 90-104; Coverage: 12%)
Gene names: MJ0970, cbiX, cfbA
Sequence domains: CbiX

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P31
Unit cell:
a: 50.21Å b: 50.21Å c: 90.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.193 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Two Distinct Thermodynamic Gradients for Cellular Metalation of Vitamin B12.
Young et al. (2023)