Research workbench
Solution structure of a bacterial cyclic nucleotide-activated K+ channel binding domain in complex with camp
Analyse Solution structure of a bacterial cyclic nucleotide-activated K+ channel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K0G
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MLL3241 protein
- UniProt
- Q98GN8
- Ligands
- CMP
- Pockets
- 1 · best druggability 0.53
Structure
solution nmr · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MLL3241 protein | protein | 142 | 37% helix, 25% strand | Q98GN8 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.53 | 0.81 | 22 | CMP |
Compared structures
- 2K0G · Solution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain… · the same entry in another collection · chain A against A, TM-score 1.00
- Q98GN8 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated potassium channel MLL3241… · a predicted model of the same protein · chain A against A, TM-score 0.88
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 Q98GN8
- Elsewhere: RCSB PDB 2K0G · PDBe 2K0G · UniProt Q98GN8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.