Research workbench
Crystal structure of MthK gating ring in a ligand-free form
Analyse Crystal structure of MthK gating ring in a ligand-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RO0
- Type
- protein
- Length
- 8,840 residues
- Chains
- 40
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.18
- Source
- Methanothermobacter thermautotrophicus
- Molecule
- Calcium-gated potassium channel MthK
- UniProt
- O27564
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · resolution 3.18 · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, a, B, b, C, c, D, d, E, e, F, f, G, g, H, h, I, i, J, j, K, k, L, l, M, m, N, n, O, o, P, p, Q, q, R, r, S, s, T, t | Calcium-gated potassium channel MthK | protein | 221 | 38% helix, 23% 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 | 649 | 0.77 | 0.83 | 75 | empty |
| 2 | 481 | 0.77 | 0.85 | 45 | empty |
| 3 | 1157 | 0.76 | 0.79 | 154 | empty |
| 4 | 892 | 0.75 | 0.79 | 72 | empty |
| 5 | 881 | 0.74 | 0.79 | 114 | empty |
Interfaces
95 interfaces between chains.
- J–j · 3810 Ų buried · 60 hydrogen bonds · protein-protein
- Q–q · 3783 Ų buried · 51 hydrogen bonds · protein-protein
- K–k · 3776 Ų buried · 54 hydrogen bonds · protein-protein
- I–i · 3766 Ų buried · 50 hydrogen bonds · protein-protein
- M–m · 3761 Ų buried · 55 hydrogen bonds · protein-protein
Compared structures
- 4RO0 · Crystal structure of mthk gating ring in a ligand-free form · 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 4RO0 · PDBe 4RO0 · UniProt O27564
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