1QUV

CRYSTAL STRUCTURE OF THE RNA DIRECTED RNA POLYMERASE OF HEPATITIS C VIRUS

PDB DOI: https://doi.org/10.2210/pdb1QUV/pdb

Classification: TRANSFERASE
Organism(s): Hepacivirus hominis
Expression System: Escherichia coli BL21(DE3)
Mutation(s): Yes

Deposited: 1999-07-04 Released: 1999-11-05
Deposition Author(s): Ago, H., Miyano, M., Adachi, T., Habuka, N.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.316
R-Value Work: 0.223
R-Value Observed: 0.223

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus.

Ago, H., Adachi, T., Yoshida, A., Yamamoto, M., Habuka, N., Yatsunami, K., Miyano, M.

(1999) Structure 7: 1417-1426

PubMed: 10574802 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(00)80031-3
Primary Citation of Related Structures:
1QUV

PubMed Abstract:
Hepatitis C virus (HCV) is the major etiological agent of hepatocellular carcinoma, and HCV RNA-dependent RNA polymerase (RdRp) is one of the main potential targets for anti-HCV agents. HCV RdRp performs run-off copying replication in an RNA-selective manner for the template-primer duplex and the substrate, but the structural basis of this reaction mechanism has still to be elucidated.

Organizational Affiliation

Central Pharmaceutical Research Institute, Japan Tobacco Inc., Takatsuki, 569-1125, Japan.

Macromolecule Content

Total Structure Weight: 64.25 kDa
Atom Count: 4,580
Modelled Residue Count: 553
Deposited Residue Count: 578
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
PROTEIN (RNA-DIRECTED RNA POLYMERASE)	A	578	Hepacivirus hominis	Mutation(s): 1 EC: 2.7.7.48
UniProt
Find proteins for P26663 (Hepatitis C virus genotype 1b (isolate BK)) Explore P26663 Go to UniProtKB: P26663
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P26663
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.316
R-Value Work: 0.223
R-Value Observed: 0.223
Space Group: P 4₃ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 63.65	α = 90
b = 63.65	β = 90
c = 262.9	γ = 90

Software Package:

Software Name	Purpose
SHARP	phasing
MLPHARE	phasing
X-PLOR	refinement
DENZO	data reduction
CCP4	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1999-11-05

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1999-11-05
Type: Initial release
Version 1.1: 2008-04-27
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2018-03-14
Changes: Database references
Version 1.4: 2024-02-14
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.