MolNFT v1 · #161175 · protein
Pore-modulating toxins exploit inherent slow inactivation to block K+ channels
6Q61 · Kunitz-type conkunitzin-S1: “Pore-modulating toxins exploit inherent slow inactivation to block K+ channels”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #161175 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Q61
- Type
- protein
- Length
- 59 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kunitz-type conkunitzin-S1
- UniProt
- P0C1X2
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kunitz-type conkunitzin-S1 | protein | 59 | 22% helix, 25% strand | P0C1X2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6Q61 · 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 0.95
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 6Q61 · PDBe 6Q61 · UniProt P0C1X2
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