MolNFT v1 · #189668 · protein
Structure of apo-HSTRPM2 channel tm domain
7VQ2 · Transient receptor potential cation channel subfamily M…: “Structure of apo-HSTRPM2 channel tm domain”. Electron microscopy, 20 pockets (best druggability 0.89). MolNFT v1 #189668 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7VQ2
- Type
- protein
- Length
- 1,416 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transient receptor potential cation channel subfamily M member 2
- UniProt
- O94759
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily M member 2 | protein | 354 | 69% helix, 0% strand | O94759 |
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 | 1006 | 0.89 | 0.90 | 128 | empty |
| 2 | 772 | 0.84 | 0.86 | 73 | empty |
| 3 | 321 | 0.78 | 0.88 | 42 | empty |
| 4 | 323 | 0.77 | 0.88 | 40 | empty |
| 5 | 337 | 0.77 | 0.87 | 40 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2877 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 2875 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 2874 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 2870 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 830 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 O94759
- Elsewhere: RCSB PDB 7VQ2 · PDBe 7VQ2 · UniProt O94759
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