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Photosynthetic reaction center from rhodopseudomonas viridis (qb- depleted)

Analyse Photosynthetic reaction center from rhodopseudomonas viridis (qb- depleted) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PRC
Type
protein
Length
1,186 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Photosynthetic reaction center
UniProt
P07173, P06009, P06010, P06008
Ligands
HEM, BCB, BPB, MQ7, NS5, FE2, SO4
Pockets
20 · best druggability 0.88

Structure

x-ray diffraction · 4 distinct chains · 50% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CPhotosynthetic reaction centerprotein33243% helix, 4% strandP07173
LPhotosynthetic reaction centerprotein27366% helix, 4% strandP06009
MPhotosynthetic reaction centerprotein32363% helix, 5% strandP06010
HPhotosynthetic reaction centerprotein25826% helix, 24% strandP06008

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains C, L, M
  • BCB · Bacteriochlorophyll B · ligand · 4 copies · chains L, M
  • BPB · Bacteriopheophytin B · ligand · 2 copies · chains L, M
  • MQ7 · Menaquinone-7 · ligand · chains L, M
  • NS5 · 15-cis-1,2-dihydroneurosporene · ligand · chains M
  • FE2 · Fe (II) ion · metal · chains L, M
  • SO4 · Sulfate ion · ion · 4 copies · chains L, M, H
  • LDA · Lauryl dimethylamine-N-oxide · additive · 7 copies · chains L, M, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18570.880.90104HEM
28440.840.8579BCB
31000.770.9831empty
42190.740.8838MQ7
5580.720.9922empty

Interfaces

6 interfaces between chains.

  • L–M · 4394 Ų buried · 62 hydrogen bonds · protein-protein
  • M–H · 2884 Ų buried · 47 hydrogen bonds · protein-protein
  • C–M · 2742 Ų buried · 37 hydrogen bonds · protein-protein
  • L–H · 1865 Ų buried · 25 hydrogen bonds · protein-protein
  • C–L · 1775 Ų buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor, 1 modified (heme attachment, formylation).

Compared structures

  • 3PRC · Photosynthetic reaction center from rhodopseudomonas viridis (qb-depleted) · the same entry in another collection · chain H against H, TM-score 1.00
  • P07173 · AlphaFold monomer V2.0 prediction for photosynthetic reaction center cytochrome C subunit… · a predicted model of the same protein · chain C against A, TM-score 1.00
  • P06009 · AlphaFold monomer V2.0 prediction for reaction center protein L chain (P06009) · a predicted model of the same protein · chain L against A, TM-score 0.99
  • P06010 · AlphaFold monomer V2.0 prediction for reaction center protein M chain (P06010) · a predicted model of the same protein · chain M against A, TM-score 0.97
  • P06008 · AlphaFold monomer V2.0 prediction for reaction center protein H chain (P06008) · a predicted model of the same protein · chain H against A, TM-score 0.94

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