Research workbench
The crystal structure of full-length kcsa in its closed conformation
Analyse The crystal structure of full-length kcsa in its closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EFF
- Type
- protein
- Length
- 1,424 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab; Voltage-gated potassium channel
- UniProt
- P0A334
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 21% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Fab | protein | 215 | 5% helix, 42% strand | — |
| B, D | Fab | protein | 219 | 5% helix, 40% strand | — |
| K, L, M, N | Voltage-gated potassium channel | protein | 139 | 72% helix, 0% strand | P0A334 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.85 | 0.89 | 53 | empty |
| 2 | 1050 | 0.78 | 0.80 | 54 | empty |
| 3 | 177 | 0.68 | 0.87 | 26 | empty |
| 4 | 67 | 0.61 | 0.91 | 23 | empty |
| 5 | 64 | 0.61 | 0.91 | 20 | empty |
Interfaces
14 interfaces between chains.
- C–D · 1786 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1771 Ų buried · 10 hydrogen bonds · protein-protein
- K–L · 1717 Ų buried · 20 hydrogen bonds · protein-protein
- M–N · 1688 Ų buried · 14 hydrogen bonds · protein-protein
- K–N · 1534 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 3EFF · The Crystal Structure of Full-Length KcsA in its Closed Conformation · the same entry in another collection · chain C against C, 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 3EFF · PDBe 3EFF · UniProt P0A334
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