6ys9

X-ray diffraction
1.64Å resolution

T_926 truncate of ChlH from Thermosynechococcus elongatus at 1.64 A resolution

Released:
Model geometry
Fit model/data
Primary publication:
The active site of magnesium chelatase.
Nat Plants 6 1491-1502 (2020)
PMID: 33257858

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
magnesium chelatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 410 amino acids
Theoretical weight: 46.09 KDa
Source organism: Thermosynechococcus vestitus BP-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DM52 (Residues: 926-1326; Coverage: 30%)
Gene name: chlH
Sequence domains: CobN/Magnesium Chelatase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 76.48Å b: 140.33Å c: 78.01Å
α: 90° β: 108.66° γ: 90°
R-values:
R R work R free
0.203 0.201 0.247
Expression system: Escherichia coli