MolNFT v1 · #165755 · protein
Calcium-bound mthk gating ring state 2
6U5N · Calcium-gated potassium channel mthk: “Calcium-bound mthk gating ring state 2”. Electron microscopy, 1 ligand (CA), 20 pockets (best druggability 0.70). MolNFT v1 #165755 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6U5N
- 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 0.70
Structure
electron microscopy · 1 distinct chain · 39% 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 | 39% 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.70 | 0.82 | 43 | CA |
| 2 | 364 | 0.70 | 0.82 | 44 | CA |
| 3 | 273 | 0.67 | 0.83 | 40 | empty |
| 4 | 261 | 0.64 | 0.82 | 39 | CA |
| 5 | 356 | 0.55 | 0.75 | 48 | CA |
Interfaces
12 interfaces between chains.
- A–E · 3593 Ų buried · 39 hydrogen bonds · protein-protein
- C–G · 3585 Ų buried · 39 hydrogen bonds · protein-protein
- B–F · 3535 Ų buried · 37 hydrogen bonds · protein-protein
- D–H · 3531 Ų buried · 37 hydrogen bonds · protein-protein
- F–C · 776 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6U5N · Calcium-bound MthK gating ring 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 6U5N · PDBe 6U5N · UniProt O27564
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