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UniProt Q3J170

Reaction center protein H chain (Q3J170)

Reaction center protein H chain (UniProt Q3J170): 11 experimental structures on GenesisL1, 6 ligands bound, 24 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q3J170
Protein
Reaction center protein H chain
Experimental structures
11
Predicted models
0
Ligands
6
Pockets
24 · 3 records with a druggable one

Structures

11 records of Q3J170 in the MolNFT archive: 11 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
5LRIPhotosynthetic reaction center mutant with GLUL212 replaced with TRP (chain L, EL212W)x-ray diffractionHCDL—
5LRIPhotosynthetic reaction center mutant with GLUL212 replaced with TRP (chain L, EL212W)x-ray diffractionHCDL—
7P2CF(M197)H mutant structure of photosynthetic reaction center from rhodobacter sphaeroides strain rv…x-ray diffractionHNKP—
7PILCryo-EM structure of the Rhodobacter sphaeroides RC-LH1-PufXY monomer complex at 2.5 Aelectron microscopyH3PE, CD4—
7VB9Rba sphaeroides PufY-KO RC-LH1 dimer type-2electron microscopyH, hPC1, CDL10 (best 0.82)
7VNMRba sphaeroides PufY-KO RC-LH1 monomerelectron microscopyHCDL, PC16 (best 0.79)
7VNMRba sphaeroides pufy-ko rc-LH1 monomerelectron microscopyHCDL, PC1—
7VNYRba sphaeroides wt rc-LH1 monomerelectron microscopyHCDL, PC1—
7VORThe structure of dimeric photosynthetic RC-LH1 supercomplex in Class-1electron microscopyH, hPC1, CDL, SPO8 (best 0.81)
7VOYRba sphaeroides pufx-ko rc-LH1electron microscopyH——
Q3J170AlphaFold monomer V2.0 prediction for reaction center protein H chain (Q3J170)———

Ligands

  • CDL · Cardiolipin · in 7 records
  • PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · in 5 records
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · in 1 record
  • CD4 · (2R,5R,11R,14R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-2,14-bis(tetradecanoyloxy)-4,6,10,12,16-pentaoxa-5,11-diphosphatriacont-1-yl tetradecanoate · in 1 record
  • NKP · (2R)-2-hydroxy-3-(phosphonooxy)propyl (9E)-octadec-9-enoate · in 1 record
  • SPO · Spheroidene · in 1 record

Elsewhere

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