Research workbench
Human connexin 26 dodecamer at 20MMHG PCO2, PH7.4
Analyse Human connexin 26 dodecamer at 20MMHG PCO2, PH7.4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QET
- Type
- protein
- Length
- 2,256 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gap junction beta-2 protein
- UniProt
- P29033
- Ligands
- PTY
- Pockets
- 20 · best druggability 0.85
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 beta-2 protein | protein | 188 | 70% helix, 5% strand | P29033 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · 12 copies · chains A, F, B, C, D, E, G, L, H, I, J, K
- LMT · Dodecyl-beta-D-maltoside · additive · 48 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 879 | 0.85 | 0.87 | 100 | empty |
| 2 | 1112 | 0.83 | 0.84 | 106 | empty |
| 3 | 465 | 0.79 | 0.86 | 58 | empty |
| 4 | 445 | 0.79 | 0.87 | 46 | empty |
| 5 | 592 | 0.79 | 0.84 | 60 | empty |
Interfaces
24 interfaces between chains.
- B–C · 1477 Ų buried · 21 hydrogen bonds · protein-protein
- G–L · 1471 Ų buried · 21 hydrogen bonds · protein-protein
- I–J · 1466 Ų buried · 20 hydrogen bonds · protein-protein
- H–I · 1462 Ų buried · 18 hydrogen bonds · protein-protein
- E–F · 1461 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 disulfide (disulfide).
Compared structures
- 7QET · human Connexin 26 dodecamer at 20mmHg PCO2, pH7.4 · 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 P29033
- Elsewhere: RCSB PDB 7QET · PDBe 7QET · UniProt P29033
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