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Crystal structure of photosynthetic reaction center from a thermophilic bacterium, thermochromatium tepidum

Analyse Crystal structure of photosynthetic reaction center from a thermophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EYS
Type
protein
Length
1,146 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Photosynthetic reaction center
UniProt
Q93RD8
Ligands
BGL, HEM, BCL, BPH, MQ8, CRT, PEF, FE
Pockets
19 · best druggability 0.87

Structure

x-ray diffraction · 4 distinct chains · 48% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CPhotosynthetic reaction centerprotein31044% helix, 5% strand—
LPhotosynthetic reaction centerprotein28063% helix, 4% strand—
MPhotosynthetic reaction centerprotein31858% helix, 3% strand—
HPhotosynthetic reaction centerprotein23823% helix, 22% strandQ93RD8

Ligands and binding sites

  • BGL · 2-O-octyl-beta-D-glucopyranose · ligand · 6 copies · chains L, M, H, C
  • HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains C, L, M
  • BCL · Bacteriochlorophyll A · ligand · 4 copies · chains L, M
  • BPH · Bacteriopheophytin A · ligand · 2 copies · chains L, M
  • MQ8 · Menaquinone 8 · ligand · chains L, M
  • CRT · Spirilloxanthin · ligand · chains M
  • PEF · Di-palmitoyl-3-sn-phosphatidylethanolamine · ligand · chains L, M, H
  • FE · Fe (III) ion · metal · chains L, M
  • LDA · Lauryl dimethylamine-N-oxide · additive · chains L

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

Pockets

19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110160.870.87120HEM
28850.830.8581BCL
33230.760.8865empty
410390.760.7874empty
51290.720.9224empty

Interfaces

6 interfaces between chains.

  • L–M · 4552 Ų buried · 52 hydrogen bonds · protein-protein
  • M–H · 2667 Ų buried · 36 hydrogen bonds · protein-protein
  • C–M · 1968 Ų buried · 26 hydrogen bonds · protein-protein
  • L–H · 1698 Ų buried · 22 hydrogen bonds · protein-protein
  • C–L · 1409 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor (heme attachment).

Compared structures

  • 1EYS · Crystal structure of photosynthetic reaction center from a thermophilic bacterium… · the same entry in another collection · chain C against C, TM-score 1.00

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