Research workbench
Calcium-bound mthk gating ring state 1
Analyse Calcium-bound mthk gating ring state 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U5P
- Type
- protein
- Length
- 1,776 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Ligands
- CA
- Pockets
- 20 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, B, F, C, G, D, H | Calcium-gated potassium channel mthk | protein | 222 | 38% helix, 22% strand | O27564 |
Ligands and binding sites
- CA · Calcium ion · metal · 24 copies · chains A, E, B, F, C, G, D, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.72 | 0.84 | 40 | CA |
| 2 | 332 | 0.72 | 0.85 | 36 | CA |
| 3 | 381 | 0.70 | 0.82 | 44 | CA |
| 4 | 368 | 0.68 | 0.81 | 39 | CA |
| 5 | 185 | 0.46 | 0.75 | 44 | CA |
Interfaces
12 interfaces between chains.
- A–E · 3675 Ų buried · 39 hydrogen bonds · protein-protein
- C–G · 3674 Ų buried · 39 hydrogen bonds · protein-protein
- D–H · 3613 Ų buried · 37 hydrogen bonds · protein-protein
- B–F · 3607 Ų buried · 38 hydrogen bonds · protein-protein
- E–B · 737 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6U5P · Calcium-bound MthK gating ring state 1 · 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 6U5P · PDBe 6U5P · UniProt O27564
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