Research workbench
Domain IV of human calpain 13
Analyse Domain IV of human calpain 13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I7A
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calpain 13
- UniProt
- Q17RF0
- Ligands
- CA, SO4
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calpain 13 | protein | 157 | 62% helix, 6% strand | Q17RF0 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.36 | 0.74 | 16 | empty |
| 2 | 64 | 0.28 | 0.73 | 15 | empty |
Compared structures
- 2I7A · Domain IV of Human Calpain 13 · 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 Q17RF0
- Elsewhere: RCSB PDB 2I7A · PDBe 2I7A · UniProt Q17RF0
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