Research workbench

Crystal structure of NS3/4A protease in complex with asunaprevir

Analyse Crystal structure of NS3/4A protease in complex with asunaprevir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WF8
Type: protein
Length: 192 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3 protein
UniProt: X2G809
Ligands: 2R9, ZN, CL
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3 protein	protein	192	11% helix, 45% strand	X2G809

Ligands and binding sites

2R9 · N-(tert-butoxycarbonyl)-3-methyl-L-valyl-(4R)-4-[(7-chloro-4-methoxyisoquinolin-1-yl)oxy]-N-{(1R,2S)-1-[(cyclopropylsulfonyl)carbamoyl]-2-ethenylcyclopropyl}-L-prolinamide · ligand · chains A
ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.45	0.84	21	empty

Compared structures

4WF8 · Crystal structure of NS3/4A protease in complex with Asunaprevir · 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 X2G809
Elsewhere: RCSB PDB 4WF8 · PDBe 4WF8 · UniProt X2G809

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.