MolNFT v1 · #159325 · protein
Full-length mthk channel at 3.1 ångström resolution
6OLY · Calcium-gated potassium channel mthk: “Full-length mthk channel at 3.1 ångström resolution”. X-ray diffraction, 1 ligand (CA), 14 pockets (best druggability 0.72). MolNFT v1 #159325 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6OLY
- Type
- protein
- Length
- 1,257 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Ligands
- CA
- Pockets
- 14 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-gated potassium channel mthk | protein | 313 | 50% helix, 17% strand | O27564 |
| B | Calcium-gated potassium channel mthk | protein | 314 | 48% helix, 16% strand | O27564 |
| C | Calcium-gated potassium channel mthk | protein | 318 | 48% helix, 16% strand | O27564 |
| D | Calcium-gated potassium channel mthk | protein | 312 | 48% helix, 16% strand | O27564 |
Ligands and binding sites
- CA · Calcium ion · metal · 12 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.72 | 0.84 | 62 | empty |
| 2 | 350 | 0.66 | 0.81 | 67 | empty |
| 3 | 213 | 0.49 | 0.75 | 26 | empty |
| 4 | 130 | 0.43 | 0.76 | 15 | empty |
| 5 | 161 | 0.43 | 0.74 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–C · 738 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 337 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 308 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6OLY · Full-length MthK channel at 3.1 angstrom resolution · 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 6OLY · PDBe 6OLY · UniProt O27564
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