MolNFT v1 · #51556 · protein
Calmodulin complexed with CAV1.1 iq peptide
2VAY: “Calmodulin complexed with CAV1.1 iq peptide”. X-ray diffraction, 2 ligands (CA, CL), 1 pocket (best druggability 0.47). MolNFT v1 #51556 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2VAY
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Voltage-dependent L-type calcium channel subunit alpha-1S
- UniProt
- P62158, Q13698
- Ligands
- CA, CL
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 146 | 61% helix, 5% strand | P62158 |
| B | Voltage-dependent L-type calcium channel subunit alpha-1S | protein | 21 | 86% helix, 0% strand | Q13698 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.47 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1386 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 Q13698
- Elsewhere: RCSB PDB 2VAY · PDBe 2VAY · UniProt P62158 · UniProt Q13698
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