Research workbench
Closed-gate kcsa soaked in 1MM KCL/5MM BACL2
Analyse Closed-gate kcsa soaked in 1MM KCL/5MM BACL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W0G
- Type
- protein
- Length
- 534 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab heavy chain; Fab light chain; PH-gated potassium channel kcsa
- UniProt
- P0A334
- Ligands
- K
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fab heavy chain | protein | 219 | 4% helix, 49% strand | — |
| B | Fab light chain | protein | 212 | 6% helix, 53% strand | — |
| C | PH-gated potassium channel kcsa | protein | 103 | 75% helix, 0% strand | P0A334 |
Ligands and binding sites
- K · Potassium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 739 | 0.69 | 0.76 | 66 | empty |
| 2 | 68 | 0.51 | 0.86 | 16 | empty |
| 3 | 185 | 0.49 | 0.76 | 34 | empty |
| 4 | 101 | 0.38 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1803 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 506 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 428 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6W0G · Closed-gate KcsA soaked in 1mM KCl/5mM BaCl2 · 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 P0A334
- Elsewhere: RCSB PDB 6W0G · PDBe 6W0G · UniProt P0A334
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