Research workbench
Human TRPC5 apo state structure at 3 ångström
Analyse Human TRPC5 apo state structure at 3 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E4T
- Type
- protein
- Length
- 2,656 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UL62
- Ligands
- PTY, POV, Y01, YZY, ZN, CA
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 664 | — | Q9UL62 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · 4 copies · chains A, D, B, C
- POV · (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate · ligand · 4 copies · chains A, D, B, C
- Y01 · Cholesterol hemisuccinate · ligand · 4 copies · chains A, D, B, C
- YZY · (2S)-2-(hexadecanoyloxy)-3-hydroxypropyl (9Z)-octadec-9-enoate · ligand · 4 copies · chains A, D, B, C
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium 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
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 Q9UL62
- Elsewhere: RCSB PDB 7E4T · PDBe 7E4T · UniProt Q9UL62
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