Research workbench
Crystal structure of mthk rck domain in its ligand-free gating-ring form
Analyse Crystal structure of mthk rck domain in its ligand-free gating-ring form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FY8
- Type
- protein
- Length
- 1,776 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Pockets
- 14 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Calcium-gated potassium channel mthk | protein | 222 | 41% helix, 22% strand | O27564 |
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1161 | 0.73 | 0.77 | 142 | empty |
| 2 | 497 | 0.72 | 0.82 | 37 | empty |
| 3 | 1033 | 0.72 | 0.76 | 128 | empty |
| 4 | 475 | 0.71 | 0.81 | 36 | empty |
| 5 | 303 | 0.62 | 0.79 | 43 | empty |
Interfaces
12 interfaces between chains.
- B–C · 3797 Ų buried · 60 hydrogen bonds · protein-protein
- F–G · 3749 Ų buried · 46 hydrogen bonds · protein-protein
- G–H · 813 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 799 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 798 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2FY8 · Crystal structure of MthK rck domain in its ligand-free gating-ring form · the same entry in another collection · chain H against H, TM-score 1.00
- O27564 · AlphaFold monomer V2.0 prediction for calcium-gated potassium channel mthk (O27564) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 2FY8 · PDBe 2FY8 · UniProt O27564
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