Research workbench
Connexin-26 bound to calcium
Analyse Connexin-26 bound to calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ER7
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gap junction beta-2 protein
- UniProt
- P29033
- Ligands
- CA
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Gap junction beta-2 protein | protein | 156 | 63% helix, 6% strand | P29033 |
| A | Gap junction beta-2 protein | protein | 159 | 65% helix, 6% strand | P29033 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.43 | 0.74 | 24 | empty |
| 2 | 91 | 0.40 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- B–A · 1257 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 P29033
- Elsewhere: RCSB PDB 5ER7 · PDBe 5ER7 · UniProt P29033
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