Brand  (β version)

PDB ID: 2AX0

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Ligands
Code Name Style Show Link
SO4 Sulfate ion PoSSuM
5X 5r-(2e-methyl-3-phenyl-allyl)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2AX0   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Hepatitis C Virus NS5b RNA Polymerase in complex with a covalent inhibitor (5x)
Release Data : 2006-01-24
Compound :
mol_id molecule chains
1 Genome polyprotein A,B
ec: 2.7.7.48
fragment: NS5B RNA-directed RNA polymerase
mutation: V499A,S506N,Q514R,T520I,P540A,S543G,V552T,S563G,L564V,R566H
Source :
mol_id organism_scientific expression_system
1 Hepatitis C virus  (taxid:11103) Escherichia coli  (taxid:562)
Authors : Powers, J.P., Piper, D.E., Li, Y., Mayorga, V., Anzola, J., Chen, J.M., Jaen, J.C., Lee, G., Liu, J., Peterson, M.G., Tonn, G.R., Ye, Q., Walker, N.P., Wang, Z.
Keywords : HCV, NS5B, Polymerase, Fingers, Thumb, Palm, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

SAR and Mode of Action of Novel Non-Nucleoside Inhibitors of Hepatitis C NS5b RNA Polymerase.

Powers, J.P.,Piper, D.E.,Li, Y.  et al.
(2006)  J.Med.Chem.  49 : 1034 - 1046

PubMed: 16451069
DOI: 10.1021/jm050859x

Reaction

Chain : A, B
UniProt : P26663 (POLG_HCVBK)
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 UniProtKB:P27958
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[Serine protease/helicase NS3]
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + phosphate + H(+) 		3.6.1.15 UniProtKB:P27958
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[Serine protease/helicase NS3]
ATP + H2O = ADP + phosphate + H(+) 		3.6.4.13 UniProtKB:P27958
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[RNA-directed RNA polymerase]
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate 		2.7.7.48 PROSITE-ProRule:PRU00539, PubMed:20194503, PubMed:9343198
-
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:11591719
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:8861916
ECO:0000250 | UniProtKB:Q9WMX2
Binds 1 zinc ion which has a structural role (PubMed:8861916). The magnesium ion is essential for the helicase activity (By similarity).
Mg(2+) ECO:0000305 | PubMed:11884572
Binds 2 magnesium ion that constitute a dinuclear catalytic metal center.