Research workbench
Cryo-EM structure of the N-terminal deletion mutant of human pannexin- 1 in a nanodisc
Analyse Cryo-EM structure of the N-terminal deletion mutant of human pannexin- 1 in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WSV
- Type
- protein
- Length
- 2,051 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pannexin-1
- UniProt
- Q96RD7
- Pockets
- 20 · best druggability 0.76
Structure
electron microscopy · 1 distinct chain · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Pannexin-1 | protein | 293 | 63% helix, 4% strand | Q96RD7 |
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 | 893 | 0.76 | 0.79 | 74 | empty |
| 2 | 299 | 0.76 | 0.87 | 41 | empty |
| 3 | 1065 | 0.75 | 0.77 | 94 | empty |
| 4 | 193 | 0.75 | 0.90 | 34 | empty |
| 5 | 922 | 0.75 | 0.78 | 84 | empty |
Interfaces
7 interfaces between chains.
- E–F · 2038 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 1930 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1858 Ų buried · 6 hydrogen bonds · protein-protein
- F–G · 1837 Ų buried · 6 hydrogen bonds · protein-protein
- A–G · 1819 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
- 7WSV · Cryo-EM structure of the N-terminal deletion mutant of human pannexin-1 in a nanodisc · the same entry in another collection · chain G against G, TM-score 1.00
- Q96RD7 · AlphaFold monomer V2.0 prediction for pannexin-1 (Q96RD7) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q96RD7
- Elsewhere: RCSB PDB 7WSV · PDBe 7WSV · UniProt Q96RD7
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