Research workbench
Lipophilic envelope-spanning tunnel B (letb), model 4
Analyse Lipophilic envelope-spanning tunnel B (letb), model 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V0F
- Type
- protein
- Length
- 2,106 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intermembrane transport protein yebt
- UniProt
- P76272
- Pockets
- 20 · best druggability 0.68
Structure
electron microscopy · 1 distinct chain · 12% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Intermembrane transport protein yebt | protein | 351 | 12% helix, 41% strand | P76272 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 546 | 0.68 | 0.78 | 64 | empty |
| 2 | 445 | 0.68 | 0.80 | 69 | empty |
| 3 | 509 | 0.67 | 0.78 | 59 | empty |
| 4 | 466 | 0.66 | 0.78 | 55 | empty |
| 5 | 455 | 0.66 | 0.79 | 52 | empty |
Interfaces
6 interfaces between chains.
- E–F · 1900 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1897 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1896 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1895 Ų buried · 15 hydrogen bonds · protein-protein
- A–F · 1893 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6V0F · Lipophilic Envelope-spanning Tunnel B (LetB), Model 4 · the same entry in another collection · chain C against C, TM-score 1.00
- P76272 · AlphaFold monomer V2.0 prediction for intermembrane transport protein yebt (P76272) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P76272
- Elsewhere: RCSB PDB 6V0F · PDBe 6V0F · UniProt P76272
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