MolNFT v1 · #182534 · protein
Kcsa open gate E71V mutant in potassium
7MUB · Fab heavy chain: “Kcsa open gate E71V mutant in potassium”. X-ray diffraction, 1 ligand (K), 4 pockets (best druggability 0.58). MolNFT v1 #182534 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7MUB
- Type
- protein
- Length
- 493 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 0.58
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fab heavy chain | protein | 208 | 3% helix, 45% strand | — |
| B | Fab light chain | protein | 194 | 7% helix, 43% strand | — |
| C | PH-gated potassium channel kcsa | protein | 91 | 71% helix, 0% strand | P0A334 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · 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 | 86 | 0.58 | 0.87 | 21 | empty |
| 2 | 385 | 0.54 | 0.73 | 54 | empty |
| 3 | 120 | 0.38 | 0.74 | 26 | empty |
| 4 | 58 | 0.28 | 0.73 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1645 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 450 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 387 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7MUB · KcsA Open gate E71V mutant in Potassium · 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 7MUB · PDBe 7MUB · UniProt P0A334
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