Research workbench

Hepatitis C virus NS3 proteinase

Analyse Hepatitis C virus NS3 proteinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1A1Q
Type: protein
Length: 531 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3 proteinase
UniProt: P26663
Ligands: ZN
Pockets: 8 · best druggability 0.38

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3 proteinase	protein	183	0% helix, 0% strand	P26663
B	NS3 proteinase	protein	170	0% helix, 0% strand	P26663
C	NS3 proteinase	protein	178	0% helix, 0% strand	P26663

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A, B, C

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

Pockets

8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.38	0.73	30	empty
2	90	0.35	0.72	28	empty
3	80	0.35	0.73	26	empty
4	80	0.34	0.73	21	empty
5	64	0.33	0.74	18	empty

Interfaces

2 interfaces between chains.

A–C · 308 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 80 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1A1Q · Hepatitis C virus NS3 proteinase · 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 P26663
Elsewhere: RCSB PDB 1A1Q · PDBe 1A1Q · UniProt P26663

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