MolNFT v1 · #8896 · protein

Structure of the hepatitis C virus RNA helicase domain

1HEI · HCV helicase: “Structure of the hepatitis C virus RNA helicase domain”. X-ray diffraction, 1 ligand (CA), 5 pockets (best druggability 0.84). MolNFT v1 #8896 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HCV helicase	protein	443	33% helix, 20% strand	P27958
B	HCV helicase	protein	412	32% helix, 17% strand	P27958

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1083	0.84	0.85	119	empty
2	182	0.71	0.89	35	empty
3	125	0.40	0.75	24	empty
4	57	0.38	0.80	18	empty
5	67	0.33	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1027 Å² 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

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 P27958
Elsewhere: RCSB PDB 1HEI · PDBe 1HEI · UniProt P27958

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