Research workbench
Crystal Structure of calmodulin complexed with a peptide
Analyse Crystal Structure of calmodulin complexed with a peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EWT
- Type
- protein
- Length
- 159 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Calmodulin; Tumor necrosis factor receptor superfamily member 6
- UniProt
- P62158, P25445
- Ligands
- CA
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · resolution 2.4 · 2 distinct chains · 62% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 145 | 60% helix, 6% strand | P62158 |
| E | Tumor necrosis factor receptor superfamily member 6 | protein | 14 | 79% helix, 0% strand | P25445 |
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 | 111 | 0.49 | 0.80 | 26 | empty |
Interfaces
1 interface between chains.
- A–E · 1155 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3EWT · Crystal structure of calmodulin complexed with a peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P25445 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member 6… · a predicted model of the same protein · chain E against A, TM-score 0.70
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 P25445
- Elsewhere: RCSB PDB 3EWT · PDBe 3EWT · UniProt P62158 · UniProt P25445
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