Research workbench
Structure of calmodulin complexed with a fragment of the olfactory cng channel
Analyse Structure of calmodulin complexed with a fragment of the olfactory cng channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SY9
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Cyclic-nucleotide-gated olfactory channel
- UniProt
- P62155, Q03041
- Ligands
- CA
- Pockets
- 2 · best druggability 0.69
Structure
solution nmr · 2 distinct chains · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 148 | 62% helix, 3% strand | P62155 |
| B | Cyclic-nucleotide-gated olfactory channel | protein | 19 | 84% helix, 0% strand | Q03041 |
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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 303 | 0.69 | 0.83 | 46 | empty |
| 2 | 108 | 0.53 | 0.82 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1271 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1SY9 · Structure of calmodulin complexed with a fragment of the olfactory CNG channel · the same entry in another collection · chain A against A, TM-score 1.00
- Q03041 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated olfactory channel (Q03041) · a predicted model of the same protein · chain B against A, TM-score 0.45
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 P62155
- Every structure of UniProt Q03041
- Elsewhere: RCSB PDB 1SY9 · PDBe 1SY9 · UniProt P62155 · UniProt Q03041
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