MolNFT v1 · #44208 · protein
3D structure of calmodulin and calmodulin binding domain of olfactory cyclic nucleotide-gated ion channel complex
2M0J: “3D structure of calmodulin and calmodulin binding domain of olfactory cyclic nucleotide-gated ion channel…”. Solution nmr, 1 ligand (CA), 2 pockets (best druggability 0.56). MolNFT v1 #44208 on GenesisL1: 3D structure, binding sites…
- PDB
- 2M0J
- Type
- protein
- Length
- 176 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Peptide from cyclic nucleotide-gated olfactory channel
- UniProt
- P62158, Q00195
- Ligands
- CA
- Pockets
- 2 · best druggability 0.56
Structure
solution nmr · 2 distinct chains · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 148 | 58% helix, 5% strand | P62158 |
| B | Peptide from cyclic nucleotide-gated olfactory channel | protein | 28 | 61% helix, 0% strand | Q00195 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.56 | 0.80 | 28 | empty |
| 2 | 65 | 0.41 | 0.81 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1723 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2M0J · 3D Structure of Calmodulin and Calmodulin binding domain of Olfactory cyclic… · the same entry in another collection · chain A against A, TM-score 1.00
- Q00195 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated olfactory channel (Q00195) · a predicted model of the same protein · chain B against A, TM-score 0.57
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 P62158
- Every structure of UniProt Q00195
- Elsewhere: RCSB PDB 2M0J · PDBe 2M0J · UniProt P62158 · UniProt Q00195
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