Research workbench
Cryo-EM structure of human TRPC3 at 4.36A resolution
Analyse Cryo-EM structure of human TRPC3 at 4.36A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZBG
- Type
- protein
- Length
- 2,680 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 0.85
Structure
electron microscopy · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Short transient receptor potential channel 3 | protein | 670 | 68% helix, 0% strand | Q13507 |
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 | 784 | 0.85 | 0.88 | 91 | empty |
| 2 | 1198 | 0.84 | 0.84 | 121 | empty |
| 3 | 696 | 0.84 | 0.87 | 78 | empty |
| 4 | 650 | 0.84 | 0.88 | 76 | empty |
| 5 | 603 | 0.82 | 0.87 | 70 | empty |
Interfaces
6 interfaces between chains.
- A–B · 4137 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 4135 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 4135 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 4129 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 57 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5ZBG · Cryo-EM structure of human TRPC3 at 4.36A resolution · 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 0.96
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 Q13507
- Elsewhere: RCSB PDB 5ZBG · PDBe 5ZBG · UniProt Q13507
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