Research workbench

Hepatitis C virus NS5B RNA-dependent RNA polymerase

Analyse Hepatitis C virus NS5B RNA-dependent RNA polymerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C2P
Type: protein
Length: 1,119 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-dependent RNA polymerase
EC: 2.7.7.48
UniProt: P26663
Pockets: 15 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-dependent RNA polymerase (EC 2.7.7.48)	protein	558	50% helix, 15% strand	P26663
B	RNA-dependent RNA polymerase (EC 2.7.7.48)	protein	561	49% helix, 16% strand	P26663

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1097	0.80	0.81	88	empty
2	1092	0.80	0.81	80	empty
3	1140	0.76	0.79	68	empty
4	118	0.51	0.81	21	empty
5	102	0.51	0.82	17	empty

Interfaces

1 interface between chains.

A–B · 555 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 modified (engineered).

Compared structures

1C2P · Hepatitis C virus NS5B RNA-dependent RNA polymerase · 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 1C2P · PDBe 1C2P · UniProt P26663

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