Research workbench
cryo-EM structure of human Pannexin 1 channel
Analyse cryo-EM structure of human Pannexin 1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M02
- Type
- protein
- Length
- 2,345 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Homo sapiens
- Molecule
- Pannexin-1
- UniProt
- Q96RD7
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · resolution 3.2 · 1 distinct chain · 51% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Pannexin-1 | protein | 335 | 51% 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 | 85 | 0.77 | 0.98 | 19 | empty |
| 2 | 762 | 0.77 | 0.81 | 82 | empty |
| 3 | 89 | 0.77 | 0.98 | 19 | empty |
| 4 | 175 | 0.77 | 0.93 | 25 | empty |
| 5 | 756 | 0.77 | 0.81 | 76 | empty |
Interfaces
7 interfaces between chains.
- A–G · 2880 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 2878 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 2876 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 2874 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 2872 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
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 Q96RD7
- Elsewhere: RCSB PDB 6M02 · PDBe 6M02 · UniProt Q96RD7
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