Research workbench
Structure of the mouse TRPC4 ion channel
Analyse Structure of the mouse TRPC4 ion channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z96
- Type
- protein
- Length
- 2,665 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Short transient receptor potential channel 4
- UniProt
- Q9QUQ5
- Ligands
- Y01, LPP, NA
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 61% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Short transient receptor potential channel 4 | protein | 670 | 61% helix, 1% strand | Q9QUQ5 |
| B, C, D | Short transient receptor potential channel 4 | protein | 665 | 61% helix, 1% strand | Q9QUQ5 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 4 copies · chains A, D, B, C
- LPP · 2-(hexadecanoyloxy)-1-[(phosphonooxy)methyl]ethyl hexadecanoate · ligand · 4 copies · chains A, D, B, C
- NA · Sodium ion · metal · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 635 | 0.86 | 0.90 | 48 | NA |
| 2 | 1095 | 0.84 | 0.84 | 107 | empty |
| 3 | 1080 | 0.83 | 0.84 | 98 | empty |
| 4 | 1089 | 0.83 | 0.83 | 74 | NA |
| 5 | 1044 | 0.83 | 0.84 | 96 | empty |
Interfaces
6 interfaces between chains.
- A–B · 5180 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 5143 Ų buried · 33 hydrogen bonds · protein-protein
- B–C · 5108 Ų buried · 35 hydrogen bonds · protein-protein
- A–D · 5092 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 98 Ų buried · 0 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 Q9QUQ5
- Elsewhere: RCSB PDB 5Z96 · PDBe 5Z96 · UniProt Q9QUQ5
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