Research workbench
Crystal structure of CA2+/CAM-CAV2.2 iq domain (without cloning artifact, hm to tv) complex
Analyse Crystal structure of CA2+/CAM-CAV2.2 iq domain (without cloning artifact, hm to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DVJ
- Type
- protein
- Length
- 161 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Voltage-dependent N-type calcium channel subunit alpha-1B
- UniProt
- P62158, Q05152
- Ligands
- CA
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 140 | 60% helix, 4% strand | P62158 |
| B | Voltage-dependent N-type calcium channel subunit alpha-1B | protein | 21 | 67% helix, 0% strand | Q05152 |
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
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 | 70 | 0.29 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1355 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3DVJ · Crystal Structure of Ca2+/CaM-CaV2.2 IQ domain (without cloning artifact, HM to TV)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q05152 · AlphaFold monomer V2.0 prediction for voltage-dependent N-type calcium channel subunit… · a predicted model of the same protein · chain B against A, TM-score 0.54
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 Q05152
- Elsewhere: RCSB PDB 3DVJ · PDBe 3DVJ · UniProt P62158 · UniProt Q05152
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