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- PDB-2wcx: Crystal Structure of Hepatitis C Virus NS5B Polymerase in Complex... -
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Basic information
Entry | Database: PDB / ID: 2wcx | ||||||
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Title | Crystal Structure of Hepatitis C Virus NS5B Polymerase in Complex with Thienopyrrole-Based Finger-Loop Inhibitors | ||||||
![]() | RNA-DIRECTED RNA POLYMERASE | ||||||
![]() | HYDROLASE / ENVELOPE PROTEIN / HEPATITIS C VIRUS / RNA-DEPENDENT RNA-POLYMERASE / NUCLEOTIDE-BINDING / ALLOSTERIC INHIBITOR / NON NUCLEOSIDE INHIBITOR / NNI / HCV / NS5B / MEMBRANE / HELICASE / POLYMERASE / ATP-BINDING / RNA-BINDING / GENOTYPE 1B / VIRAL PROTEIN / TRANSMEMBRANE / RNA REPLICATION | ||||||
Function / homology | ![]() hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / SH3 domain binding / nucleoside-triphosphate phosphatase ...hepacivirin / host cell mitochondrial membrane / host cell lipid droplet / symbiont-mediated suppression of host TRAF-mediated signal transduction / transformation of host cell by virus / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / SH3 domain binding / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / viral nucleocapsid / clathrin-dependent endocytosis of virus by host cell / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / host cell perinuclear region of cytoplasm / host cell endoplasmic reticulum membrane / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA helicase / ribonucleoprotein complex / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / host cell nucleus / virion attachment to host cell / host cell plasma membrane / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Di Marco, S. | ||||||
![]() | ![]() Title: Optimization of Thienopyrrole-Based Finger-Loop Inhibitors of the Hepatitis C Virus Ns5B Polymerase. Authors: Martin Hernando, J.I. / Ontoria, J.M. / Malancona, S. / Attenni, B. / Fiore, F. / Bonelli, F. / Koch, U. / Di Marco, S. / Colarusso, S. / Ponzi, S. / Gennari, N. / Vignetti, S.E. / Del ...Authors: Martin Hernando, J.I. / Ontoria, J.M. / Malancona, S. / Attenni, B. / Fiore, F. / Bonelli, F. / Koch, U. / Di Marco, S. / Colarusso, S. / Ponzi, S. / Gennari, N. / Vignetti, S.E. / Del Rosario Rico Ferreira, M. / Habermann, J. / Rowley, M. / Narjes, F. #1: ![]() Title: Interdomain Communication in Hepatitis C Virus Polymerase Abolished by Small Molecule Inhibitors Bound to a Novel Allosteric Site. Authors: Di Marco, S. / Volpari, C. / Tomei, L. / Altamura, S. / Harper, S. / Narjes, F. / Koch, U. / Rowley, M. / De Francesco, R. / Migliaccio, G. / Carfi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 126.4 KB | Display | ![]() |
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PDB format | ![]() | 96.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 774.3 KB | Display | ![]() |
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Full document | ![]() | 786.4 KB | Display | |
Data in XML | ![]() | 27.2 KB | Display | |
Data in CIF | ![]() | 40.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1csjS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 59772.711 Da / Num. of mol.: 1 / Fragment: NS5B, RESIDUES 2420-2955 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-VGC / | #4: Water | ChemComp-HOH / | Sequence details | NS5B PROTEIN, GENOTYPE 1B AND STRAIN BK, LACKING THE C- TERMINAL 55 AMINO ACIDS. TOTAL AMINO ACIDS ...NS5B PROTEIN, GENOTYPE 1B AND STRAIN BK, LACKING THE C- TERMINAL 55 AMINO ACIDS. TOTAL AMINO ACIDS 535, UNIPROT REFERENCE P26663, 2420-2955 | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.41 % / Description: NONE |
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Crystal grow | pH: 6 / Details: pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 2→33.71 Å / Num. obs: 42683 / % possible obs: 97.2 % / Observed criterion σ(I): 2 / Redundancy: 6.9 % / Biso Wilson estimate: 21.65 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 18 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 5.2 / % possible all: 94.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1CSJ Resolution: 2→95.35 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.926 / SU B: 5.099 / SU ML: 0.146 / Cross valid method: THROUGHOUT / ESU R: 0.159 / ESU R Free: 0.146 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. NO ELECTRON DENSITY WAS PRESENT FOR RESIDUES 22-35, 148-152 AND 532-536 WHICH WERE THEREFORE EXCLUDED FROM THE REFINEMENT. IN ADDITION, ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. NO ELECTRON DENSITY WAS PRESENT FOR RESIDUES 22-35, 148-152 AND 532-536 WHICH WERE THEREFORE EXCLUDED FROM THE REFINEMENT. IN ADDITION, SIDE CHAIN DENSITY FOR RESIDUES GLU18, LYS20 AND LEU21 WAS MISSING AND THEREFORE THESE RESIDUES HAVE BEEN MODELED AS ALANINE.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.471 Å2
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Refinement step | Cycle: LAST / Resolution: 2→95.35 Å
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