Research workbench
M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand selectivity, cyclic-gmp bound
Analyse M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MUV
- Type
- protein
- Length
- 281 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic nucleotide-gated potassium channel MLL3241
- UniProt
- Q98GN8
- Ligands
- PCG, NA
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic nucleotide-gated potassium channel MLL3241 | protein | 142 | 44% helix, 25% strand | Q98GN8 |
| B | Cyclic nucleotide-gated potassium channel MLL3241 | protein | 139 | 42% helix, 25% strand | Q98GN8 |
Ligands and binding sites
- PCG · Cyclic guanosine monophosphate · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.65 | 0.89 | 20 | PCG |
| 2 | 122 | 0.63 | 0.88 | 24 | PCG |
| 3 | 363 | 0.57 | 0.75 | 44 | empty |
Interfaces
1 interface between chains.
- A–B · 749 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4MUV · M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand selectivity… · 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 B against A, TM-score 0.96
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 4MUV · PDBe 4MUV · UniProt Q98GN8
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