Research workbench
The 1.65 ångström structure of calmodulin RS20 peptide complex
Analyse The 1.65 ångström structure of calmodulin RS20 peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QTX
- Type
- protein
- Length
- 168 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.65
- Source
- Escherichia coli; SYNTHETIC CONSTRUCT
- Molecule
- Protein (calmodulin); Protein (RS20)
- UniProt
- P11799
- Ligands
- CA
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · resolution 1.65 · 2 distinct chains · 60% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (calmodulin) | protein | 148 | 57% helix, 5% strand | — |
| B | Protein (RS20) | protein | 20 | 80% helix, 0% strand | P11799 |
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
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.41 | 0.75 | 20 | empty |
| 2 | 91 | 0.41 | 0.78 | 22 | empty |
| 3 | 50 | 0.29 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1618 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 1QTX · The 1.65 ångström structure of calmodulin RS20 peptide complex · the same entry in another collection · chain A against A, TM-score 1.00
- P11799 · AlphaFold monomer V2.0 prediction for myosin light chain kinase, smooth muscle (P11799) · a predicted model of the same protein · chain B against A, TM-score 0.61
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 P11799
- Elsewhere: RCSB PDB 1QTX · PDBe 1QTX · UniProt P11799
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