Research workbench
Cryoem structure of the caveolin-1 8S complex
Analyse Cryoem structure of the caveolin-1 8S complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SC0
- Type
- protein
- Length
- 1,419 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caveolin-1
- UniProt
- Q03135
- Pockets
- 20 · best druggability 0.44
Structure
electron microscopy · 1 distinct chain · 64% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K | Caveolin-1 | protein | 129 | 64% helix, 5% strand | Q03135 |
Pockets
20 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.44 | 0.81 | 18 | empty |
| 2 | 84 | 0.42 | 0.79 | 18 | empty |
| 3 | 103 | 0.40 | 0.76 | 23 | empty |
| 4 | 114 | 0.39 | 0.75 | 20 | empty |
| 5 | 70 | 0.39 | 0.79 | 17 | empty |
Interfaces
22 interfaces between chains.
- D–E · 3217 Ų buried · 11 hydrogen bonds · protein-protein
- I–J · 3215 Ų buried · 11 hydrogen bonds · protein-protein
- F–G · 3215 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 3213 Ų buried · 12 hydrogen bonds · protein-protein
- A–K · 3210 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 Q03135
- Elsewhere: RCSB PDB 7SC0 · PDBe 7SC0 · UniProt Q03135
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