Research workbench
HCN2J 443-645 in the presence of cgmp
Analyse HCN2J 443-645 in the presence of cgmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q3E
- Type
- protein
- Length
- 381 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2
- UniProt
- O88703
- Ligands
- PCG
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2 | protein | 192 | 53% helix, 20% strand | O88703 |
| B | POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2 | protein | 189 | 55% helix, 20% strand | O88703 |
Ligands and binding sites
- PCG · Cyclic guanosine monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.59 | 0.85 | 18 | PCG |
| 2 | 104 | 0.58 | 0.85 | 21 | PCG |
| 3 | 175 | 0.52 | 0.79 | 24 | empty |
| 4 | 188 | 0.46 | 0.74 | 22 | empty |
| 5 | 161 | 0.44 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 570 Ų buried · 1 hydrogen bond · 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 O88703
- Elsewhere: RCSB PDB 1Q3E · PDBe 1Q3E · UniProt O88703
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