Research workbench
Lipophilic envelope-spanning tunnel B (letb), model 2
Analyse Lipophilic envelope-spanning tunnel B (letb), model 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V0D
- Type
- protein
- Length
- 4,992 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 0.83
Structure
electron microscopy · 1 distinct chain · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Intermembrane transport protein yebt | protein | 832 | 10% helix, 37% strand | P76272 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.83 | 0.84 | 153 | empty |
| 2 | 880 | 0.81 | 0.83 | 100 | empty |
| 3 | 286 | 0.72 | 0.86 | 47 | empty |
| 4 | 344 | 0.70 | 0.83 | 49 | empty |
| 5 | 239 | 0.69 | 0.86 | 38 | empty |
Interfaces
6 interfaces between chains.
- B–C · 4872 Ų buried · 37 hydrogen bonds · protein-protein
- A–F · 4870 Ų buried · 37 hydrogen bonds · protein-protein
- D–E · 4870 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 4865 Ų buried · 37 hydrogen bonds · protein-protein
- E–F · 4849 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 6V0D · Lipophilic Envelope-spanning Tunnel B (LetB), Model 2 · 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 0.80
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 6V0D · PDBe 6V0D · UniProt P76272
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