Research workbench
Mthk N-terminal truncation rck domain state 2 bound with calcium
Analyse Mthk N-terminal truncation rck domain 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
- 6UX4
- 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 0.69
Structure
electron microscopy · 1 distinct chain · 37% 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 | 37% 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.69 | 0.83 | 38 | CA |
| 2 | 297 | 0.69 | 0.83 | 33 | CA |
| 3 | 96 | 0.55 | 0.85 | 22 | CA |
| 4 | 98 | 0.52 | 0.83 | 25 | empty |
| 5 | 125 | 0.47 | 0.79 | 20 | CA |
Interfaces
14 interfaces between chains.
- A–E · 3652 Ų buried · 36 hydrogen bonds · protein-protein
- C–G · 3636 Ų buried · 38 hydrogen bonds · protein-protein
- B–F · 3615 Ų buried · 34 hydrogen bonds · protein-protein
- D–H · 3601 Ų buried · 31 hydrogen bonds · protein-protein
- F–C · 786 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6UX4 · MthK N-terminal truncation RCK domain 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 6UX4 · PDBe 6UX4 · UniProt O27564
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