Research workbench
Cryoem structure of xenopus KCNQ1 channel
Analyse Cryoem structure of xenopus KCNQ1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VMS
- Type
- protein
- Length
- 484 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily kqt member 1; Calmodulin
- UniProt
- P70057, P62158
- Ligands
- CA
- Pockets
- 5 · best druggability 0.57
Structure
electron microscopy · 2 distinct chains · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium voltage-gated channel subfamily kqt member 1 | protein | 343 | 80% helix, 1% strand | P70057 |
| B | Calmodulin | protein | 141 | 65% helix, 3% strand | P62158 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.57 | 0.85 | 19 | empty |
| 2 | 285 | 0.53 | 0.75 | 30 | empty |
| 3 | 172 | 0.51 | 0.78 | 34 | empty |
| 4 | 93 | 0.44 | 0.80 | 21 | empty |
| 5 | 76 | 0.35 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2406 Ų buried · 11 hydrogen bonds · protein-protein
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 P70057
- Every structure of UniProt P62158
- Elsewhere: RCSB PDB 5VMS · PDBe 5VMS · UniProt P70057 · UniProt P62158
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