Research workbench
Structure of TAX-4_R421W w/cGMP open state
Analyse Structure of TAX-4_R421W w/cGMP open state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N15
- Type
- protein
- Length
- 2,080 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Caenorhabditis elegans
- Molecule
- Cyclic nucleotide-gated cation channel
- UniProt
- Q03611
- Ligands
- CPL, PCG, PX2
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · resolution 2.9 · 1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cyclic nucleotide-gated cation channel | protein | 520 | 53% helix, 12% strand | Q03611 |
Ligands and binding sites
- CPL · 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine · ligand · 20 copies · chains A, B, C, D
- PCG · Cyclic guanosine monophosphate · ligand · 4 copies · chains A, B, C, D
- PX2 · 1,2-dilauroyl-sn-glycero-3-phosphate · ligand · 4 copies · chains A, D, 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 | 1040 | 0.80 | 0.82 | 61 | empty |
| 2 | 697 | 0.71 | 0.78 | 71 | empty |
| 3 | 611 | 0.69 | 0.78 | 60 | empty |
| 4 | 590 | 0.69 | 0.78 | 60 | empty |
| 5 | 471 | 0.69 | 0.80 | 55 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2782 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 2772 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 2770 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 2762 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 24 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 Q03611
- Elsewhere: RCSB PDB 7N15 · PDBe 7N15 · UniProt Q03611
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