Research workbench
Composite MAP of human KV1.3 channel in apo state with beta subunits
Analyse Composite MAP of human KV1.3 channel in apo state with beta subunits in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WF3
- Type
- protein
- Length
- 2,744 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22001, Q13303
- Ligands
- NAP, K
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, D, F, H | — | protein | 252 | — | P22001 |
| C, G, I, M | — | protein | 328 | — | Q13303 |
| J, N, O, P | — | protein | 106 | — | P22001 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains C, G, I, M
- K · Potassium ion · metal · 4 copies · chains B, D, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WF3 · Composite map of human Kv1.3 channel in apo state with beta subunits · the same entry in another collection · chain P against P, 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 P22001
- Every structure of UniProt Q13303
- Elsewhere: RCSB PDB 7WF3 · PDBe 7WF3 · UniProt P22001 · UniProt Q13303
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