Brand  (β version)

PDB ID: 2DXS

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Ligands
Code Name Style Show Link
JTP N-[(13-cyclohexyl-6,7-dihydroindolo[1,2-D][1,4]benzoxazepin-10-yl)carbonyl]-2-methyl-L-alanine PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2DXS   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Crystal structure of HCV NS5B RNA polymerase complexed with a tetracyclic inhibitor
Release Data : 2006-12-26
Compound :
mol_id molecule chains synonym
1 Genome polyprotein A,B NS5B, p68
ec: 2.7.7.48
fragment: RNA-directed RNA polymerase, RESIDUES 2419-2962
Source :
mol_id organism_scientific expression_system
1 Hepatitis C virus  (taxid:11103) Escherichia coli BL21(DE3)  (taxid:469008)
strain: BK
gene: 1B
expression_system_strain: BL21 (DE3)
expression_system_vector_type: T7
expression_system_plasmid: pET17b
Authors : Adachi, T., Tsuruha, J., Doi, S., Murase, K., Ikegashira, K., Watanabe, S., Uehara, K., Orita, T., Nomura, A., Kamada, M.
Keywords : HCV, NS5B, RNA polymerase, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

Discovery of Conformationally Constrained Tetracyclic Compounds as Potent Hepatitis C Virus NS5B RNA Polymerase Inhibitors

Ikegashira, K.,Oka, T.,Hirashima, S.  et al.
(2006)  J.Med.Chem.  49 : 6950 - 6953

PubMed: 17125247
DOI: 10.1021/jm0610245

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
-
[Serine protease/helicase NS3]
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + phosphate + H(+) 		3.6.1.15 UniProtKB:P27958
-
[Serine protease/helicase NS3]
ATP + H2O = ADP + phosphate + H(+) 		3.6.4.13 UniProtKB:P27958
-
[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.