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UniProt Q99AU2

HCV Polymerase (Q99AU2)

HCV Polymerase (UniProt Q99AU2): 34 experimental structures on GenesisL1, 2 ligands bound, 23 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q99AU2
Protein
HCV Polymerase
Experimental structures
34
Predicted models
0
Ligands
2
Pockets
23 · 2 records with a druggable one

Structures

34 records of Q99AU2 in the MolNFT archive: 34 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2D3UX-ray crystal structure of hepatitis C virus RNA dependent RNA polymerase in complex with…x-ray diffractionA, B——
2D3UX-ray crystal structure of hepatitis C virus RNA dependent RNA polymerase in complex with…x-ray diffractionA, B——
2D3ZX-ray crystal structure of hepatitis C virus RNA-dependent RNA polymerase in complex with…x-ray diffractionA, B——
2D3ZX-ray crystal structure of hepatitis C virus RNA-dependent RNA polymerase in complex with…x-ray diffractionA, B——
2D41X-ray crystal structure of hepatitis C virus RNA-dependent RNA polymerase in complex with…x-ray diffractionA, B——
2D41X-ray crystal structure of hepatitis C virus RNA-dependent RNA polymerase in complex with…x-ray diffractionA, B——
2GC8Structure of a Proline Sulfonamide Inhibitor Bound to HCV NS5b Polymerasex-ray diffractionA, B——
2GC8Structure of a proline sulfonamide inhibitor bound to HCV NS5B polymerasex-ray diffractionA, B——
2IJNIsothiazoles as active-site inhibitors of HCV NS5B polymerasex-ray diffractionA, B——
2IJNIsothiazoles as active-site inhibitors of HCV NS5B polymerasex-ray diffractionA, B——
2QE2Structure of HCV NS5B Bound to an Anthranilic Acid Inhibitorx-ray diffractionA, B——
2QE2Structure of HCV NS5B bound to an anthranilic acid inhibitorx-ray diffractionA, B——
2QE5Structure of HCV NS5B Bound to an Anthranilic Acid Inhibitorx-ray diffractionA, B, C, D——
2QE5Structure of HCV NS5B bound to an anthranilic acid inhibitorx-ray diffractionA, B, C, D——
2ZKUStructure of hepatitis C virus NS5B polymerase in a new crystal formx-ray diffractionA, B, C, D——
2ZKUStructure of hepatitis C virus NS5B polymerase in a new crystal formx-ray diffractionA, B, C, D——
3CWJCrystal structure of hcv ns5b polymerase with a novel pyridazi inhibitorx-ray diffractionA, B——
3CWJCrystal structure of HCV NS5B polymerase with a novel pyridazinone inhibitorx-ray diffractionA, B——
3HHKHCV NS5b polymerase complex with a substituted benzothiadizinex-ray diffractionA, B——
3HHKHCV NS5B polymerase complex with a substituted benzothiadizinex-ray diffractionA, B——
3O8BVisualizing ATP-dependent RNA Translocation by the NS3 Helicase from HCVx-ray diffractionA, B——
3O8BVisualizing ATP-dependent RNA translocation by the NS3 helicase from HCVx-ray diffractionA, B——
3O8CVisualizing ATP-dependent RNA Translocation by the NS3 Helicase from HCVx-ray diffractionA, B——
3O8CVisualizing ATP-dependent RNA translocation by the NS3 helicase from HCVx-ray diffractionA, B——
3O8DVisualizing ATP-dependent RNA Translocation by the NS3 Helicase from HCVx-ray diffractionA, B——
3O8DVisualizing ATP-dependent RNA translocation by the NS3 helicase from HCVx-ray diffractionA, B——
3O8RVisualizing ATP-dependent RNA Translocation by the NS3 Helicase from HCVx-ray diffractionA, B——
3O8RVisualizing ATP-dependent RNA translocation by the NS3 helicase from HCVx-ray diffractionA, B——
3UDL3-heterocyclyl quinolone bound to HCV NS5Bx-ray diffractionA, B, C, D——
3UDL3-heterocyclyl quinolone bound to HCV NS5Bx-ray diffractionA, B, C, D——
6MVKHCV NS5B 1b N316 bound to Compound 18x-ray diffractionA, BK4J11 (best 0.81)
6MVKHCV NS5B 1B N316 bound to compound 18x-ray diffractionA, BK4J—
6MVQHCV NS5B 1b N316 bound to Compound 31x-ray diffractionA, BK4M12 (best 0.81)
6MVQHCV NS5B 1B N316 bound to compound 31x-ray diffractionA, BK4M—

Ligands

  • K4J · (4-{(4S)-3-[5-cyclopropyl-2-(4-fluorophenyl)-3-(methylcarbamoyl)-1-benzofuran-6-yl]-2-oxo-1,3-oxazolidin-4-yl}-2-fluorophenyl)boronic acid · in 2 records
  • K4M · (4-{1-[5-cyclopropyl-2-(4-fluorophenyl)-3-(methylcarbamoyl)-1-benzofuran-6-yl]-1H-1,2,4-triazol-5-yl}-2-fluorophenyl)boronic acid · in 2 records

Elsewhere

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