MolNFT v1 · #5982 · protein
Crystal structure of photosynthetic reaction center from a thermophilic bacterium, thermochromatium tepidum
1EYS: “Crystal structure of photosynthetic reaction center from a thermophilic bacterium, thermochromatium tepidum”. X-ray diffraction, 8 ligands (BGL, HEM, BCL), 19 pockets (best druggability 0.87). MolNFT v1 #5982 on GenesisL1: 3D…
- 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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Photosynthetic reaction center | protein | 310 | 44% helix, 5% strand | — |
| L | Photosynthetic reaction center | protein | 280 | 63% helix, 4% strand | — |
| M | Photosynthetic reaction center | protein | 318 | 58% helix, 3% strand | — |
| H | Photosynthetic reaction center | protein | 238 | 23% helix, 22% strand | Q93RD8 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1016 | 0.87 | 0.87 | 120 | HEM |
| 2 | 885 | 0.83 | 0.85 | 81 | BCL |
| 3 | 323 | 0.76 | 0.88 | 65 | empty |
| 4 | 1039 | 0.76 | 0.78 | 74 | empty |
| 5 | 129 | 0.72 | 0.92 | 24 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q93RD8
- Elsewhere: RCSB PDB 1EYS · PDBe 1EYS · UniProt Q93RD8
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