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Structure of hetero complex of non structural protein (ns) of hepatitis C virus (HCV) and synthetic peptidic compound

Analyse Structure of hetero complex of non structural protein (ns) of hepatitis C virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DXW
Type: protein
Length: 165 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease
UniProt: P90191
Ligands: 2ZF, ZN
Pockets: 1 · best druggability 0.57

Structure

solution nmr · 1 distinct chain · 12% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease	protein	165	12% helix, 38% strand	P90191

Ligands and binding sites

2ZF · N-(tert-butoxycarbonyl)-L-alpha-glutamyl-N-[(1R)-1-(carboxycarbonyl)-3,3-difluoropropyl]-L-leucinamide · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.57	0.87	30	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

1DXW · structure of hetero complex of non structural protein (NS) of hepatitis C virus (HCV) and… · 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 P90191
Elsewhere: RCSB PDB 1DXW · PDBe 1DXW · UniProt P90191

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