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X-ray crystal structure of NS3 helicase from HCV with a bound fragment inhibitor at 2.08 a resolution

Analyse X-ray crystal structure of NS3 helicase from HCV with a bound fragment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WXP
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3-4 protease
UniProt: K7XFN2
Ligands: 3VY, NA, CL
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3-4 protease	protein	445	34% helix, 21% strand	K7XFN2

Ligands and binding sites

3VY · (1-methyl-1H-indol-3-yl)acetic acid · ligand · chains A
NA · Sodium 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	328	0.54	0.74	34	empty
2	73	0.35	0.76	17	3VY
3	60	0.33	0.76	10	empty

Compared structures

4WXP · X-ray crystal structure of NS3 Helicase from HCV with a bound fragment inhibitor at 2.08… · 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 K7XFN2
Elsewhere: RCSB PDB 4WXP · PDBe 4WXP · UniProt K7XFN2

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