Research workbench
Crystal structure of human caspase-1 (CYS285->ala, CYS362->ala, CYS364->ala, CYS397->ala) in complex with 1-methyl-3-trifluoromethyl- 1H-THIENO[2,3-C]PYRAZOLE-5-carboxylic acid (2-mercapto-ethyl)-amide
Analyse Crystal structure of human caspase-1 (CYS285->ala, CYS362->ala, CYS364->ala… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FQQ
- Type
- protein
- Length
- 235 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
- F1G
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-1 (EC 3.4.22.36) | protein | 147 | 29% helix, 24% strand | P29466 |
| B | Caspase-1 (EC 3.4.22.36) | protein | 88 | 26% helix, 13% strand | P29466 |
Ligands and binding sites
- F1G · 1-methyl-3-trifluoromethyl-1H-thieno[2,3-c]pyrazole-5-carboxylic acid (2-mercapto-ethyl)-amide · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.56 | 0.84 | 31 | empty |
| 2 | 52 | 0.40 | 0.81 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1933 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2FQQ · Crystal structure of human caspase-1 (Cys285->Ala, Cys362->Ala, Cys364->Ala, Cys397->Ala)… · the same entry in another collection · chain A against A, TM-score 1.00
- P29466 · AlphaFold monomer V2.0 prediction for caspase-1 (P29466) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 2FQQ · PDBe 2FQQ · UniProt P29466
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