3njr

X-ray diffraction
2.7Å resolution

Crystal structure of C-terminal domain of precorrin-6Y C5,15-methyltransferase from Rhodobacter capsulatus

Released:

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + precorrin-6B = S-adenosyl-L-homocysteine + precorrin-7 + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-112679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetrapyrrole methylase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 204 amino acids
Theoretical weight: 22.02 KDa
Source organism: Rhodobacter capsulatus SB 1003
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D5AV04 (Residues: 214-396; Coverage: 46%)
Gene names: RCAP_rcc02042, cobL
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 114.354Å b: 44.799Å c: 84.11Å
α: 90° β: 119.75° γ: 90°
R-values:
R R work R free
0.189 0.185 0.265
Expression system: Escherichia coli BL21(DE3)