Research workbench
Mthk N-terminal truncation state 2 bound with calcium
Analyse Mthk N-terminal truncation state 2 bound with calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UXA
- Type
- protein
- Length
- 2,104 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B, D | Calcium-gated potassium channel mthk | protein | 304 | 49% helix, 16% strand | O27564 |
| E, G, F, H | Calcium-gated potassium channel mthk | protein | 222 | 35% helix, 22% 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 | 1113 | 0.84 | 0.85 | 158 | empty |
| 2 | 1169 | 0.80 | 0.81 | 131 | empty |
| 3 | 819 | 0.78 | 0.81 | 140 | empty |
| 4 | 534 | 0.77 | 0.85 | 104 | empty |
| 5 | 580 | 0.77 | 0.84 | 77 | empty |
Interfaces
14 interfaces between chains.
- A–E · 1023 Ų buried · 0 hydrogen bonds · protein-protein
- D–H · 1022 Ų buried · 0 hydrogen bonds · protein-protein
- B–F · 1021 Ų buried · 0 hydrogen bonds · protein-protein
- C–G · 1018 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 310 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6UXA · MthK N-terminal truncation state 2 bound with calcium · 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 6UXA · PDBe 6UXA · UniProt O27564
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