Research workbench
Structure of TRPC3 gain of function mutation R803C at 3.2 ångström in 1340NM free calcium state
Analyse Structure of TRPC3 gain of function mutation R803C at 3.2 ångström in 1340NM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DXE
- Type
- protein
- Length
- 2,740 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Short transient receptor potential channel 3
- UniProt
- Q13507
- Ligands
- Y01, POV, 98R, ZN
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A, B, C | Short transient receptor potential channel 3 | protein | 685 | 67% helix, 1% strand | Q13507 |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 8 copies · chains D, A, C, B
- POV · (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate · ligand · 4 copies · chains D, B, A, C
- 98R · [(2S)-2-[(E)-octadec-10-enoyl]oxy-3-oxidanyl-propyl] octadec-10-enoate · ligand · 4 copies · chains D, B, A, C
- ZN · Zinc ion · metal · 4 copies · chains D, A, B, C
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 | 859 | 0.85 | 0.86 | 82 | empty |
| 2 | 884 | 0.78 | 0.81 | 72 | empty |
| 3 | 906 | 0.78 | 0.80 | 76 | empty |
| 4 | 647 | 0.77 | 0.82 | 67 | empty |
| 5 | 1183 | 0.75 | 0.77 | 85 | empty |
Interfaces
6 interfaces between chains.
- D–A · 3101 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 3097 Ų buried · 13 hydrogen bonds · protein-protein
- D–B · 3094 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 3091 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 36 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7DXE · Structure of TRPC3 gain of function mutation R803C at 3.2 angstrom in 1340nM free calcium… · the same entry in another collection · chain D against D, 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 D against A, TM-score 0.98
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 7DXE · PDBe 7DXE · UniProt Q13507
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