MolNFT v1 · #185336 · protein
Ligand-bound human KV3.1 cryo-EM structure (lu AG00563)
7PQU: “Ligand-bound human KV3.1 cryo-EM structure (lu AG00563)”. Electron microscopy, 2 ligands (805, K). MolNFT v1 #185336 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7PQU
- Type
- protein
- Length
- 1,312 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P48547
- Ligands
- 805, K
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 328 | — | P48547 |
Ligands and binding sites
- 805 · 1-(4-methylphenyl)sulfonyl-N-(1,3-oxazol-2-ylmethyl) pyrrole-3-carboxamide · ligand · 4 copies · chains A, B, C, D
- K · Potassium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PQU · Ligand-bound human Kv3.1 cryo-EM structure (Lu AG00563) · the same entry in another collection · chain A against A, TM-score 1.00
- P48547 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily C member… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P48547
- Elsewhere: RCSB PDB 7PQU · PDBe 7PQU · UniProt P48547
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