Research workbench
Cryo-EM structure of human TRPV6-Y467A in amphipols
Analyse Cryo-EM structure of human TRPV6-Y467A in amphipols in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D7S
- Type
- protein
- Length
- 2,372 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily V member 6
- UniProt
- Q9H1D0
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 55% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily V member 6 | protein | 593 | 55% helix, 2% strand | Q9H1D0 |
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 | 1164 | 0.85 | 0.86 | 81 | empty |
| 2 | 686 | 0.76 | 0.81 | 44 | empty |
| 3 | 677 | 0.76 | 0.81 | 48 | empty |
| 4 | 685 | 0.76 | 0.81 | 44 | empty |
| 5 | 695 | 0.76 | 0.81 | 47 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3426 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 3413 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 3383 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 3348 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 27 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 Q9H1D0
- Elsewhere: RCSB PDB 6D7S · PDBe 6D7S · UniProt Q9H1D0
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