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Identification of novel allosteric inhibitors of hepatitis C virus NS5B polymerase thumb domain (site II) by structure-based design

Analyse Identification of novel allosteric inhibitors of hepatitis C virus NS5B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WRM
Type: protein
Length: 531 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-directed RNA polymerase
EC: 2.7.7.48
UniProt: P26663
Ligands: QQ3
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-directed RNA polymerase (EC 2.7.7.48)	protein	531	51% helix, 15% strand	P26663

Ligands and binding sites

QQ3 · (3R)-3-(4-methyl-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl)hexanoic acid · ligand · 3 copies · chains A

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

Pockets

8 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	874	0.73	0.77	82	empty
2	117	0.50	0.80	17	empty
3	67	0.39	0.79	17	empty
4	114	0.39	0.75	25	empty
5	84	0.35	0.76	12	empty

Compared structures

2WRM · Identification of Novel Allosteric Inhibitors of Hepatitis C Virus NS5B Polymerase Thumb… · 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 2WRM · PDBe 2WRM · UniProt P26663

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