Research workbench
Distal C2-like domain of human calpain-7
Analyse Distal C2-like domain of human calpain-7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QFE
- Type
- protein
- Length
- 139 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calpain-7
- EC
- 3.4.22.-
- UniProt
- Q9Y6W3
- Ligands
- BR
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calpain-7 (EC 3.4.22.-) | protein | 139 | 4% helix, 50% strand | Q9Y6W3 |
Ligands and binding sites
- BR · Bromide ion · ion · 18 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q9Y6W3
- Elsewhere: RCSB PDB 2QFE · PDBe 2QFE · UniProt Q9Y6W3
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