Research workbench
Procaspase-1 zymogen domain crystal structure
Analyse Procaspase-1 zymogen domain crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E4C
- Type
- protein
- Length
- 540 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-1
- EC
- 3.4.22.36
- UniProt
- P29466
- Ligands
- MG
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-1 (EC 3.4.22.36) | protein | 271 | 31% helix, 20% strand | P29466 |
| B | Caspase-1 (EC 3.4.22.36) | protein | 269 | 32% helix, 20% strand | P29466 |
Ligands and binding sites
- MG · Magnesium ion · metal · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.68 | 0.80 | 41 | empty |
| 2 | 301 | 0.66 | 0.82 | 41 | empty |
| 3 | 304 | 0.56 | 0.76 | 32 | MG |
| 4 | 154 | 0.54 | 0.81 | 40 | empty |
| 5 | 174 | 0.51 | 0.78 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 2041 Ų buried · 83 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 P29466
- Elsewhere: RCSB PDB 3E4C · PDBe 3E4C · UniProt P29466
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