MolNFT v1 · #53605 · protein

Insertion mutant E173GP174 of the NS3 protease-helicase from dengue virus

2WZQ: “Insertion mutant E173GP174 of the NS3 protease-helicase from dengue virus”. X-ray diffraction, 1 ligand (CL), 6 pockets (best druggability 0.82). MolNFT v1 #53605 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2WZQ
Type: protein
Length: 594 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NS3 protease-helicase
UniProt: Q2TN89
Ligands: CL
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NS3 protease-helicase	protein	581	25% helix, 24% strand	Q2TN89
C	NS3 protease-helicase	protein	13	0% helix, 31% strand	Q2TN89

Ligands and binding sites

CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1078	0.82	0.83	92	CL, GOL
2	609	0.70	0.79	67	empty
3	63	0.51	0.86	20	empty
4	131	0.46	0.78	22	empty
5	61	0.42	0.82	12	empty

Interfaces

1 interface between chains.

A–C · 932 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2WZQ · Insertion Mutant E173GP174 of the NS3 protease-helicase from dengue virus · 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 Q2TN89
Elsewhere: RCSB PDB 2WZQ · PDBe 2WZQ · UniProt Q2TN89

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