Research workbench
Cytoplasmic domain of TRPC3
Analyse Cytoplasmic domain of TRPC3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D7L
- Type
- protein
- Length
- 1,152 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Short transient receptor potential channel 3
- UniProt
- Q13507
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 1 distinct chain · 60% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Short transient receptor potential channel 3 | protein | 288 | 60% helix, 0% strand | Q13507 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1070 | 0.87 | 0.88 | 99 | empty |
| 2 | 786 | 0.83 | 0.86 | 66 | empty |
| 3 | 676 | 0.82 | 0.86 | 57 | empty |
| 4 | 590 | 0.74 | 0.81 | 55 | empty |
| 5 | 65 | 0.74 | 0.97 | 21 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1357 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1355 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1355 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1352 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 44 Ų buried · 0 hydrogen bonds · protein-protein
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 Q13507
- Elsewhere: RCSB PDB 6D7L · PDBe 6D7L · UniProt Q13507
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