Research workbench
Calcium-bound mthk open-inactivated state 2
Analyse Calcium-bound mthk open-inactivated state 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U6E
- Type
- protein
- Length
- 2,118 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 3 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, C | Calcium-gated potassium channel mthk | protein | 304 | 45% helix, 14% strand | O27564 |
| B | Calcium-gated potassium channel mthk | protein | 318 | 47% helix, 15% strand | O27564 |
| H, G, F, E | Calcium-gated potassium channel mthk | protein | 222 | 32% helix, 21% strand | O27564 |
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 | 939 | 0.82 | 0.83 | 144 | empty |
| 2 | 629 | 0.78 | 0.84 | 116 | empty |
| 3 | 822 | 0.77 | 0.81 | 89 | empty |
| 4 | 586 | 0.77 | 0.84 | 74 | empty |
| 5 | 566 | 0.77 | 0.84 | 77 | empty |
Interfaces
14 interfaces between chains.
- B–F · 1069 Ų buried · 0 hydrogen bonds · protein-protein
- D–H · 1066 Ų buried · 0 hydrogen bonds · protein-protein
- C–G · 1028 Ų buried · 1 hydrogen bond · protein-protein
- A–E · 1027 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 289 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6U6E · Calcium-bound MthK open-inactivated state 2 · the same entry in another collection · chain A against A, 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 O27564
- Elsewhere: RCSB PDB 6U6E · PDBe 6U6E · UniProt O27564
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