Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
9H4 Tert-butyl [(2r,6s,12z,13as,14ar,16as)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-{[(1-methylcyclopropyl)sulfonyl]carbamoyl}-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[E]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl]carbamate
EDO 1,2-ethanediol
GOL Glycerol
SO4 Sulfate ion
ZN Zinc ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 6UE3   PDBj   RCSB PDB   PDBe
Header : ANTIVIRAL PROTEIN
Title : Crystal structure of HCV NS3/4A D168A protease in complex with PC (JZ01-15)
Release Data : 2020-03-04
Compound :
mol_id molecule chains
1 NS3 protease A
Source :
mol_id organism_scientific expression_system
1 Hepacivirus C  (taxid:11103) Escherichia coli  (taxid:562)
Authors : Zephyr, J., Schiffer, C.A.
Keywords : Drug Resistance, Protease inhibitor, HYDROLASE-HYDROLASE Inhibitor complex, HYDROLASE, VIRAL PROTEIN, ANTIVIRAL PROTEIN
Exp. method : X-RAY DIFFRACTION ( 1.56 Å )
Citation :

Avoiding Drug Resistance by Substrate Envelope-Guided Design: Toward Potent and Robust HCV NS3/4A Protease Inhibitors.

Matthew, A.N.,Zephyr, J.,Nageswara Rao, D.  et al.
(2020)  Mbio  11

PubMed: 32234812
DOI: 10.1128/mBio.00172-20