Research workbench
Structure of human KCNQ1-KCNE3-cam complex
Analyse Structure of human KCNQ1-KCNE3-cam complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V00
- Type
- protein
- Length
- 2,180 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily kqt member 1; Calmodulin-1; Mcherry fluorescent…
- UniProt
- P51787, P0DP23, X5DSL3, Q9Y6H6
- Ligands
- CA
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 3 distinct chains · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Potassium voltage-gated channel subfamily kqt member 1 | protein | 354 | 73% helix, 1% strand | P51787 |
| B, E, H, K | Calmodulin-1 | protein | 144 | 60% helix, 6% strand | P0DP23 |
| C, F, I, L | Mcherry fluorescent PROTEIN,POTASSIUM voltage-gated channel subfamily E member 3 | protein | 47 | 68% helix, 0% strand | X5DSL3, Q9Y6H6 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains B, E, H, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1171 | 0.88 | 0.88 | 139 | empty |
| 2 | 564 | 0.81 | 0.87 | 60 | empty |
| 3 | 1165 | 0.70 | 0.74 | 102 | empty |
| 4 | 143 | 0.62 | 0.85 | 26 | empty |
| 5 | 413 | 0.61 | 0.76 | 54 | CA |
Interfaces
38 interfaces between chains.
- A–D · 2709 Ų buried · 14 hydrogen bonds · protein-protein
- D–G · 2708 Ų buried · 14 hydrogen bonds · protein-protein
- A–J · 2704 Ų buried · 14 hydrogen bonds · protein-protein
- G–J · 2700 Ų buried · 14 hydrogen bonds · protein-protein
- G–H · 2564 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6V00 · structure of human KCNQ1-KCNE3-CaM complex · 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 P51787
- Every structure of UniProt P0DP23
- Every structure of UniProt X5DSL3
- Every structure of UniProt Q9Y6H6
- Elsewhere: RCSB PDB 6V00 · PDBe 6V00 · UniProt P51787 · UniProt P0DP23 · UniProt X5DSL3 · UniProt Q9Y6H6
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