MolNFT v1 · #161183 · protein
Pore-modulating toxins exploit inherent slow inactivation to block K+ channels
6Q6C · Kunitz-type conkunitzin-S1: “Pore-modulating toxins exploit inherent slow inactivation to block K+ channels”. X-ray diffraction, 2 ligands (NO3, PO4), 1 pocket (best druggability 0.42). MolNFT v1 #161183 on GenesisL1: 3D structure…
- PDB
- 6Q6C
- Type
- protein
- Length
- 117 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kunitz-type conkunitzin-S1
- UniProt
- P0C1X2
- Ligands
- NO3, PO4
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kunitz-type conkunitzin-S1 | protein | 58 | 22% helix, 26% strand | P0C1X2 |
| B | Kunitz-type conkunitzin-S1 | protein | 59 | 20% helix, 25% strand | P0C1X2 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 6 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.42 | 0.78 | 19 | EDO |
Interfaces
1 interface between chains.
- A–B · 467 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6Q6C · Pore-modulating toxins exploit inherent slow inactivation to block K+ channels · the same entry in another collection · chain A against A, TM-score 1.00
- P0C1X2 · AlphaFold monomer V2.0 prediction for kunitz-type conkunitzin-S1 (P0C1X2) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P0C1X2
- Elsewhere: RCSB PDB 6Q6C · PDBe 6Q6C · UniProt P0C1X2
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