MolNFT v1 · #156879 · protein
Structure of connexin-50 intercellular gap junction channel at 3.4 ångström resolution by cryoem
6MHY · Gap junction alpha-8 protein, connexin-50: “Structure of connexin-50 intercellular gap junction channel at 3.4 ångström resolution by cryoem”. Electron microscopy, 20 pockets (best druggability 0.62). MolNFT v1 #156879 on GenesisL1…
- PDB
- 6MHY
- Type
- protein
- Length
- 2,124 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gap junction alpha-8 protein, connexin-50
- UniProt
- P55917
- Pockets
- 20 · best druggability 0.62
Structure
electron microscopy · 1 distinct chain · 70% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Gap junction alpha-8 protein, connexin-50 | protein | 177 | 70% helix, 5% strand | P55917 |
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 | 278 | 0.62 | 0.80 | 66 | empty |
| 2 | 270 | 0.60 | 0.78 | 36 | empty |
| 3 | 283 | 0.59 | 0.78 | 36 | empty |
| 4 | 271 | 0.59 | 0.78 | 37 | empty |
| 5 | 223 | 0.59 | 0.80 | 31 | empty |
Interfaces
24 interfaces between chains.
- K–L · 1413 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1412 Ų buried · 9 hydrogen bonds · protein-protein
- G–H · 1408 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1407 Ų buried · 9 hydrogen bonds · protein-protein
- A–F · 1406 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 disulfide (disulfide).
Compared structures
- 6MHY · Structure of connexin-50 intercellular gap junction channel at 3.4 angstrom resolution by… · the same entry in another collection · chain L against L, TM-score 1.00
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 P55917
- Elsewhere: RCSB PDB 6MHY · PDBe 6MHY · UniProt P55917
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