Research workbench
Composite MAP of human KV1.3 channel in dalazatide-bound state with beta subunits
Analyse Composite MAP of human KV1.3 channel in dalazatide-bound state with beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WF4
- Type
- protein
- Length
- 2,760 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 |
|---|---|---|---|---|---|
| D, B, F, H | — | protein | 256 | — | P22001 |
| G, I, M, o | — | protein | 328 | — | Q13303 |
| J, N, O, P | — | protein | 106 | — | P22001 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains G, I, M, o
- K · Potassium ion · metal · 3 copies · chains D, B, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WF4 · Composite map of human Kv1.3 channel in dalazatide-bound state with beta subunits · the same entry in another collection · chain H against H, 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 7WF4 · PDBe 7WF4 · UniProt P22001 · UniProt Q13303
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