Research workbench
A novel conformation of calmodulin
Analyse A novel conformation of calmodulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HEX
- Type
- protein
- Length
- 279 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin
- UniProt
- P62204
- Ligands
- ZN, CA
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 139 | 57% helix, 6% strand | P62204 |
| B | Calmodulin | protein | 140 | 59% helix, 6% strand | P62204 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.64 | 0.77 | 34 | empty |
| 2 | 122 | 0.43 | 0.76 | 19 | empty |
| 3 | 96 | 0.39 | 0.76 | 18 | empty |
| 4 | 53 | 0.29 | 0.75 | 16 | empty |
| 5 | 63 | 0.28 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1359 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4HEX · A novel conformation of calmodulin · the same entry in another collection · chain A against A, TM-score 1.00
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 P62204
- Elsewhere: RCSB PDB 4HEX · PDBe 4HEX · UniProt P62204
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