Research workbench
Crystal structure of a mu-like calpain
Analyse Crystal structure of a mu-like calpain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QXP
- Type
- protein
- Length
- 1,571 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mu-like calpain
- EC
- 3.4.22.52
- UniProt
- Q07009, P97571
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mu-like calpain (EC 3.4.22.52) | protein | 783 | 29% helix, 16% strand | Q07009, P97571 |
| B | Mu-like calpain (EC 3.4.22.52) | protein | 788 | 28% helix, 19% strand | Q07009, P97571 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 761 | 0.77 | 0.82 | 83 | empty |
| 2 | 629 | 0.75 | 0.81 | 93 | empty |
| 3 | 864 | 0.74 | 0.78 | 74 | empty |
| 4 | 692 | 0.72 | 0.79 | 85 | empty |
| 5 | 590 | 0.71 | 0.79 | 58 | empty |
Interfaces
1 interface between chains.
- A–B · 270 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1QXP · Crystal Structure of a mu-like calpain · the same entry in another collection · chain A against A, TM-score 1.00
- P97571 · AlphaFold monomer V2.0 prediction for calpain-1 catalytic subunit (P97571) · a predicted model of the same protein · chain A against A, TM-score 0.74
- Q07009 · AlphaFold monomer V2.0 prediction for calpain-2 catalytic subunit (Q07009) · a predicted model of the same protein · chain A against A, TM-score 0.74
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 Q07009
- Every structure of UniProt P97571
- Elsewhere: RCSB PDB 1QXP · PDBe 1QXP · UniProt Q07009 · UniProt P97571
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