Research workbench
Structure of the human TRPC3 in a lipid-occupied, closed state
Analyse Structure of the human TRPC3 in a lipid-occupied, closed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CUD
- Type
- protein
- Length
- 2,816 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Short transient receptor potential channel 3
- UniProt
- Q13507
- Ligands
- 6OE, FGJ, NAG
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Short transient receptor potential channel 3 | protein | 704 | 67% helix, 0% strand | Q13507 |
Ligands and binding sites
- 6OE · (2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl hexanoate · ligand · 4 copies · chains A, B, C, D
- FGJ · (2R)-3-hydroxypropane-1,2-diyl dihexanoate · ligand · 4 copies · chains A, D, B, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1044 | 0.83 | 0.84 | 91 | empty |
| 2 | 805 | 0.77 | 0.81 | 107 | 6OE |
| 3 | 907 | 0.77 | 0.79 | 93 | 6OE |
| 4 | 924 | 0.77 | 0.79 | 90 | 6OE |
| 5 | 630 | 0.75 | 0.81 | 80 | 6OE |
Interfaces
6 interfaces between chains.
- B–C · 2895 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 2886 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 2886 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 2870 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 22 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 6CUD · Structure of the human TRPC3 in a lipid-occupied, closed state · the same entry in another collection · chain A against A, TM-score 1.00
- Q13507 · AlphaFold monomer V2.0 prediction for short transient receptor potential channel 3… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q13507
- Elsewhere: RCSB PDB 6CUD · PDBe 6CUD · UniProt Q13507
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