3aer

X-ray diffraction
2.8Å resolution

Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-541184 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Light-independent protochlorophyllide reductase subunit N Chains: A, C
Molecule details ›
Chains: A, C
Length: 436 amino acids
Theoretical weight: 47.21 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
  • Canonical: P26164 (Residues: 2-424; Coverage: 100%)
Gene names: RCAP_rcc00665, bchN
Sequence domains: Nitrogenase component 1 type Oxidoreductase
Structure domains: Nitrogenase molybdenum iron protein domain
Light-independent protochlorophyllide reductase subunit B Chains: B, D
Molecule details ›
Chains: B, D
Length: 525 amino acids
Theoretical weight: 57.26 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
  • Canonical: P26163 (Residues: 1-525; Coverage: 100%)
Gene names: RCAP_rcc00664, bchB, bchK
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 81.418Å b: 80.941Å c: 176.728Å
α: 90° β: 100.66° γ: 90°
R-values:
R R work R free
0.19 0.187 0.237
Expression system: Escherichia coli