Research workbench
Crystal structure of human caspase-1 in complex with ac-fltd-cmk
Analyse Crystal structure of human caspase-1 in complex with ac-fltd-cmk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BZ9
- Type
- protein
- Length
- 263 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-1; Ac-fltd-cmk
- EC
- 3.4.22.36
- UniProt
- P29466
- Ligands
- ACE, 0QE
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-1 (EC 3.4.22.36) | protein | 171 | 32% helix, 18% strand | P29466 |
| B | Caspase-1 (EC 3.4.22.36) | protein | 88 | 27% helix, 17% strand | P29466 |
| C | Ac-fltd-cmk | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B, C
- 0QE · Chloromethane · ion · chains A, C
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.48 | 0.84 | 18 | empty |
| 2 | 70 | 0.35 | 0.76 | 12 | PEG |
Interfaces
3 interfaces between chains.
- A–B · 2735 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 385 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 189 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 6BZ9 · PDBe 6BZ9 · UniProt P29466
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