PDBe 1g8p

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF BCHI SUBUNIT OF MAGNESIUM CHELATASE

Released:

Function and Biology Details

Reaction catalysed:
ATP + protoporphyrin IX + Mg(2+) + H(2)O = ADP + phosphate + Mg-protoporphyrin IX + 2 H(+). 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Magnesium-chelatase 38 kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 37.95 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
  • Canonical: P26239 (Residues: 1-350; Coverage: 100%)
Gene names: RCAP_rcc00677, bchI
Sequence domains: Magnesium chelatase, subunit ChlI
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P65
Unit cell:
a: 90.259Å b: 90.259Å c: 83.716Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.214 0.247
Expression system: Escherichia coli