Brand  (β version)

PDB ID: 3OYP

Hetero Atom Contents

  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
ZN Zinc ion PoSSuM
Non-standard Residues
Code Name Show
DAL D-alanine
0Y8 (4r)-4-[(7-bromoisoquinolin-1-yl)oxy]-L-proline
0Y9 (1r,2s)-1-amino-2-ethenylcyclopropanecarboxylic acid
Glycosylation
Code Name Emphasize
Modification
Code Name Show
PPI Propanoic acid
0YA Cyclopropanesulfonamide

Structure summary

Code : 3OYP   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : HCV NS3/4A in complex with ligand 3
Release Data : 2010-12-01
Compound :
mol_id molecule chains synonym
1 Serine protease NS3 A,B Hepacivirin, NS3P, p70
ec: 3.4.21.98, 3.6.1.15, 3.6.4.13
fragment: PROTEASE/HELICASE NS3 (P70), UNP residues 1027-1213
mol_id molecule chains synonym
2 Non-structural protein 4A C,D NS4A, p8
fragment: NONSTRUCTURAL PROTEIN NS4A (P4), UNP residues 1677-1991
mol_id molecule chains
3 Peptidomimetic inhibitor E,F
Source :
mol_id organism_scientific organism_common expression_system
1 Hepatitis C virus (isolate Japanese)  (taxid:11116) HCV Escherichia coli  (taxid:562)
mol_id organism_scientific organism_common expression_system
2 Hepatitis C virus (isolate Japanese)  (taxid:11116) HCV Escherichia coli  (taxid:562)
mol_id organism_scientific
3
synthetic: yes
Authors : Hagel, M., Niu, D., St.Martin, T., Sheets, M.P., Qiao, L., Bernard, H., Karp, R.M., Zhu, Z., Labenski, M.T., Chaturvedi, P.C., Nacht, M., Westlin, W.F., Petter, R.C., Singh, J.
Keywords : SERINE PROTEASE, NS3, NS4A, HEPATITIS C VIRUS, PROTEASE INHIBITION, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.76 Å )
Citation :

Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine.

Hagel, M.,Niu, D.,St.Martin, T.  et al.
(2011)  Nat.Chem.Biol.  7 : 22 - 24

PubMed: 21113170
DOI: 10.1038/nchembio.492

Reaction

Chain : C, D
UniProt : P26662 (POLG_HCVJA)
Reaction: EC: Evidence:
Physiological Direction:
[Serine protease/helicase NS3]
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'. 		3.4.21.98 PubMed:9060645
-
[Serine protease/helicase NS3]
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + phosphate + H(+) 		3.6.1.15 PubMed:20398661
-
[Serine protease/helicase NS3]
ATP + H2O = ADP + phosphate + H(+) 		3.6.4.13 PubMed:20398661
-
[RNA-directed RNA polymerase]
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate 		2.7.7.48 PROSITE-ProRule:PRU00539, PubMed:11907226
-
Cofactor: Evidence: Note:
Zn(2+) ECO:0000250 | UniProtKB:P26663
Activity of protease NS2 is dependent on zinc ions and completely inhibited by EDTA. This is probably due to the fact that NS2 protease activity needs NS3 N-terminus that binds a zinc atom (active region NS2-3).
Mg(2+) ECO:0000269 | PubMed:9060645
ECO:0000250 | UniProtKB:Q9WMX2
Binds 1 zinc ion, which has a structural role (PubMed:9060645). The magnesium ion is essential for the helicase activity (PubMed:20398661).
Mg(2+) ECO:0000250 | UniProtKB:P26663
Binds 2 magnesium ion that constitute a dinuclear catalytic metal center.