MolNFT v1 · #185169 · protein
Human voltage-gated potassium channel KV3.1 in dimeric state (with zn)
7PHK: “Human voltage-gated potassium channel KV3.1 in dimeric state (with zn)”. Electron microscopy, 3 ligands (PCF, ZN, K). MolNFT v1 #185169 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7PHK
- Type
- protein
- Length
- 3,140 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q3KNS8
- Ligands
- PCF, ZN, K
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B, D | — | protein | 392 | — | Q3KNS8 |
| E, G, F, H | — | protein | 393 | — | Q3KNS8 |
Ligands and binding sites
- PCF · 1,2-diacyl-sn-glycero-3-phoshocholine · ligand · 16 copies · chains A, B, C, D, E, F, G, H
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
- K · Potassium ion · metal · 8 copies · chains A, C, B, D, E, G, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PHK · Human voltage-gated potassium channel Kv3.1 in dimeric state (with Zn) · the same entry in another collection · chain B against B, 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 Q3KNS8
- Elsewhere: RCSB PDB 7PHK · PDBe 7PHK · UniProt Q3KNS8
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