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Crystal structure of HCV NS5B RNA polymerase complexed with a novel non-competitive inhibitor.

Analyse Crystal structure of HCV NS5B RNA polymerase complexed with a novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OS5
Type: protein
Length: 563 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hepatitis C virus NS5B RNA polymerase
UniProt: P26663
Ligands: NH1
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hepatitis C virus NS5B RNA polymerase	protein	563	49% helix, 15% strand	P26663

Ligands and binding sites

NH1 · 3-(4-amino-2-tert-butyl-5-methyl-phenylsulfanyl)-6-cyclopentyl-4-hydroxy-6-[2-(4-hydroxy-phenyl)-ethyl]-5,6-dihydro-pyran-2-one · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1056	0.79	0.81	86	empty
2	111	0.45	0.78	18	empty
3	133	0.43	0.75	20	NH1
4	101	0.40	0.76	23	empty
5	108	0.38	0.75	23	empty

Compared structures

1OS5 · Crystal structure of HCV NS5B RNA polymerase complexed with a novel non-competitive… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P26663
Elsewhere: RCSB PDB 1OS5 · PDBe 1OS5 · UniProt P26663

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