MolNFT v1 · #25358 · protein
M.LOTI ion channel cylic nucleotide binding domain
1VP6 · Cyclic-nucleotide binding domain of mesorhizobium loti cng…: “M.LOTI ion channel cylic nucleotide binding domain”. X-ray diffraction, 2 ligands (CMP, BR), 3 pockets (best druggability 0.56). MolNFT v1 #25358 on GenesisL1: 3D…
- PDB
- 1VP6
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic-nucleotide binding domain of mesorhizobium loti cng potassium channel
- UniProt
- Q98GN8
- Ligands
- CMP, BR
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Cyclic-nucleotide binding domain of mesorhizobium loti cng potassium channel | protein | 133 | 42% helix, 25% strand | Q98GN8 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, C
- BR · Bromide ion · ion · 16 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.56 | 0.85 | 18 | CMP |
| 2 | 99 | 0.55 | 0.84 | 18 | CMP |
| 3 | 104 | 0.48 | 0.80 | 21 | BR |
Interfaces
1 interface between chains.
- A–C · 589 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1VP6 · M.loti ion channel cylic nucleotide 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 C 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 Q98GN8
- Elsewhere: RCSB PDB 1VP6 · PDBe 1VP6 · UniProt Q98GN8
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