› 1prc

X-ray diffraction
2.3Å resolution

CRYSTALLOGRAPHIC REFINEMENT AT 2.3 ANGSTROMS RESOLUTION AND REFINED MODEL OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS

Released:
DOI: 10.2210/pdb1prc/pdb
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PDB entry 1prc coloured by chain, front view.
PDB entry 1prc coloured by chain, side view.
PDB entry 1prc coloured by chain, top view.
Source organism: Blastochloris viridis
Primary publication:
Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis.
Deisenhofer J, Epp O, Sinning I, Michel H
J Mol Biol 246 429-57 (1995)
PMID: 7877166

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
PDBe Complex ID:
PDB-CPX-138851 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Photosynthetic reaction center cytochrome c subunit Chain: C
Molecule details ›
Chain: C
Length: 336 amino acids
Theoretical weight: 37.45 KDa
Source organism: Blastochloris viridis
Expression system: Not provided
UniProt:
  • Canonical: P07173 (Residues: 21-356; Coverage: 100%)
Gene names: BVIRIDIS_00500, cytC, pufC
Sequence domains: Photosynthetic reaction centre cytochrome C subunit
Structure domains: Photosynthetic Reaction Center, subunit C, domain 2
Reaction center protein L chain Chain: L
Molecule details ›
Chain: L
Length: 273 amino acids
Theoretical weight: 30.47 KDa
Source organism: Blastochloris viridis
Expression system: Not provided
UniProt:
  • Canonical: P06009 (Residues: 2-274; Coverage: 100%)
Gene name: pufL
Sequence domains: Photosynthetic reaction centre protein
Structure domains: Photosystem II protein D1-like
Reaction center protein M chain Chain: M
Reaction center protein H chain Chain: H

Ligands and Environments

9 bound ligands:
Ligand HEC 4 x HEC
Ligand BCB 4 x BCB
Ligand BPB 2 x BPB
Ligand UQ1 1 x UQ1
Ligand FE 1 x FE
Ligand SO4 7 x SO4
Ligand MQ7 1 x MQ7
Ligand NS1 1 x NS1
Ligand LDA 2 x LDA
1 modified residue:
Ligand FME 1 x FME

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P43212
Unit cell:
a: 223.5Å b: 223.5Å c: 113.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 not available not available
Expression system: Not provided

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Citations

39 review citations

Helical membrane protein folding, stability, and evolution.
Popot et al. (2000)
38 more

41 mentions without citation

The chemistry and biochemistry of heme c: functional bases for covalent attachment.
Bowman et al. (2008)
40 more

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