Research workbench
Cryo-EM structure of TRPV5 T709D in nanodiscs in the presence of calmodulin
Analyse Cryo-EM structure of TRPV5 T709D in nanodiscs in the presence of calmodulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T6R
- Type
- protein
- Length
- 2,424 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 5
- UniProt
- Q9XSM3
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 57% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 5 | protein | 606 | 57% helix, 5% strand | Q9XSM3 |
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 | 266 | 0.83 | 0.95 | 40 | empty |
| 2 | 251 | 0.80 | 0.92 | 24 | empty |
| 3 | 427 | 0.75 | 0.84 | 51 | empty |
| 4 | 425 | 0.75 | 0.84 | 51 | empty |
| 5 | 459 | 0.74 | 0.83 | 53 | empty |
Interfaces
6 interfaces between chains.
- B–D · 3408 Ų buried · 32 hydrogen bonds · protein-protein
- A–C · 3396 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 3382 Ų buried · 33 hydrogen bonds · protein-protein
- C–D · 3372 Ų buried · 32 hydrogen bonds · protein-protein
- A–D · 43 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7T6R · Cryo-EM structure of TRPV5 T709D in nanodiscs in the presence of Calmodulin · the same entry in another collection · chain A against A, TM-score 1.00
- Q9XSM3 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9XSM3
- Elsewhere: RCSB PDB 7T6R · PDBe 7T6R · UniProt Q9XSM3
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