Research workbench
Cryo-EM structure of human TRPV6 in complex with (4- PHENYLCYCLOHEXYL)PIPERAZINE inhibitor br-cis-22A
Analyse Cryo-EM structure of human TRPV6 in complex with (4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7K4C
- Type
- protein
- Length
- 2,444 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9H1D0
- Ligands
- 81F, CA
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 611 | — | Q9H1D0 |
Ligands and binding sites
- 81F · 1-(5-bromopyridin-3-yl)-4-[cis-4-(3-methylphenyl) cyclohexyl]piperazine · ligand · 5 copies · chains A, B, C, D
- CA · Calcium ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7K4C · Cryo-EM structure of human TRPV6 in complex with (4- phenylcyclohexyl)piperazine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H1D0 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9H1D0
- Elsewhere: RCSB PDB 7K4C · PDBe 7K4C · UniProt Q9H1D0
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