Research workbench
Crystal structure analysis of cryzain bound to vinyl sulfone derived inhibitor (IV)
Analyse Crystal structure analysis of cryzain bound to vinyl sulfone derived inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F2C
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cruzain
- EC
- 3.4.22.-
- UniProt
- P25779
- Ligands
- VS4
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cruzain (EC 3.4.22.-) | protein | 215 | 25% helix, 24% strand | P25779 |
Ligands and binding sites
- VS4 · 3-[[N-[4-methyl-piperazinyl]carbonyl]-phenylalaninyl-amino]-5-phenyl-pentane-1-sulfonic acid benzyloxy-amide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1F2C · Crystal structure analysis of cryzain bound to vinyl sulfone derived inhibitor (IV) · the same entry in another collection · chain A against A, TM-score 1.00
- P25779 · AlphaFold monomer V2.0 prediction for cruzipain (P25779) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P25779
- Elsewhere: RCSB PDB 1F2C · PDBe 1F2C · UniProt P25779
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