Research workbench
Crystal structure of the fenna-matthews-olson protein from chlorobaculum tepidum
Analyse Crystal structure of the fenna-matthews-olson protein from chlorobaculum tepidum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ENI
- Type
- protein
- Length
- 713 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacteriochlorophyll a protein
- UniProt
- Q46393
- Ligands
- BCL
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacteriochlorophyll a protein | protein | 357 | 18% helix, 50% strand | Q46393 |
| C | Bacteriochlorophyll a protein | protein | 356 | 17% helix, 49% strand | Q46393 |
Ligands and binding sites
- BCL · Bacteriochlorophyll A · ligand · 16 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 915 | 0.80 | 0.82 | 95 | BCL |
| 2 | 666 | 0.79 | 0.83 | 71 | BCL |
| 3 | 560 | 0.67 | 0.77 | 63 | empty |
| 4 | 231 | 0.64 | 0.82 | 29 | BCL |
| 5 | 293 | 0.63 | 0.80 | 42 | BCL |
Interfaces
1 interface between chains.
- A–C · 466 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3ENI · Crystal structure of the Fenna-Matthews-Olson Protein from Chlorobaculum Tepidum · the same entry in another collection · chain A against A, TM-score 1.00
- Q46393 · AlphaFold monomer V2.0 prediction for bacteriochlorophyll a protein (Q46393) · a predicted model of the same protein · chain C against A, 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 Q46393
- Elsewhere: RCSB PDB 3ENI · PDBe 3ENI · UniProt Q46393
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