Research workbench
Calpain domain VI with calcium bound
Analyse Calpain domain VI with calcium bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DVI
- Type
- protein
- Length
- 346 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calpain
- UniProt
- Q64537
- Ligands
- CA
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Calpain | protein | 173 | 64% helix, 6% strand | Q64537 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.77 | 0.95 | 27 | empty |
| 2 | 170 | 0.50 | 0.78 | 22 | empty |
| 3 | 155 | 0.50 | 0.78 | 21 | empty |
| 4 | 116 | 0.45 | 0.78 | 20 | empty |
| 5 | 112 | 0.44 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2201 Ų buried · 25 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 Q64537
- Elsewhere: RCSB PDB 1DVI · PDBe 1DVI · UniProt Q64537
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