Research workbench
Crystal structure of norwalk virus protease grown in the presence of aebsf
Analyse Crystal structure of norwalk virus protease grown in the presence of aebsf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FYR
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chymotrypsin-like cysteine proteinase
- UniProt
- Q83883
- Ligands
- MG, CL
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chymotrypsin-like cysteine proteinase | protein | 171 | 8% helix, 51% strand | Q83883 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2FYR · Crystal Structure of Norwalk Virus Protease grown in the presence of AEBSF · the same entry in another collection · chain A against A, TM-score 1.00
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 Q83883
- Elsewhere: RCSB PDB 2FYR · PDBe 2FYR · UniProt Q83883
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