Research workbench
Structure of a calmodulin complex
Analyse Structure of a calmodulin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BYA
- Type
- protein
- Length
- 157 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Glutamate [NMDA] receptor subunit zeta-1 peptide
- UniProt
- P62158, Q05586
- Ligands
- CA
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 137 | 59% helix, 4% strand | P62158 |
| B | Glutamate [NMDA] receptor subunit zeta-1 peptide | protein | 20 | 80% helix, 0% strand | Q05586 |
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 | 79 | 0.33 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1417 Ų buried · 10 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 Q05586
- Elsewhere: RCSB PDB 3BYA · PDBe 3BYA · UniProt P62158 · UniProt Q05586
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