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Structure of the hepatitis C virus RNA helicase domain

Analyse Structure of the hepatitis C virus RNA helicase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HEI
Type
protein
Length
855 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HCV helicase
UniProt
P27958
Ligands
CA
Pockets
5 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHCV helicaseprotein44333% helix, 20% strandP27958
BHCV helicaseprotein41232% helix, 17% strandP27958

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110830.840.85119empty
21820.710.8935empty
31250.400.7524empty
4570.380.8018empty
5670.330.7615empty

Interfaces

1 interface between chains.

  • A–B · 1027 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1HEI · Structure of the hepatitis C virus RNA helicase domain · the same entry in another collection · chain A against A, TM-score 1.00

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