Research workbench
Structure and rearrangements in the carboxy-terminal region of spih channels
Analyse Structure and rearrangements in the carboxy-terminal region of spih channels in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q0A
- Type
- protein
- Length
- 388 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
- 7 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2 | protein | 194 | 53% 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
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.65 | 0.88 | 21 | PCG |
| 2 | 276 | 0.63 | 0.81 | 28 | empty |
| 3 | 159 | 0.62 | 0.84 | 23 | PCG |
| 4 | 248 | 0.51 | 0.75 | 24 | empty |
| 5 | 226 | 0.46 | 0.73 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 589 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2Q0A · Structure and rearrangements in the carboxy-terminal region of SpIH channels · the same entry in another collection · chain B against B, TM-score 1.00
- O88703 · AlphaFold monomer V2.0 prediction for POTASSIUM/SODIUM hyperpolarization-activated cyclic… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 2Q0A · PDBe 2Q0A · UniProt O88703
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