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Dengue virus 4 NS3 helicase in complex with ADP

Analyse Dengue virus 4 NS3 helicase in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JLS
Type: protein
Length: 443 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease subunit NS3
EC: 3.4.21.91
UniProt: Q2YHF0
Ligands: ADP, MN, CL
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease subunit NS3 (EC 3.4.21.91)	protein	443	34% helix, 17% strand	Q2YHF0

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MN · Manganese (II) ion · metal · chains A
CL · Chloride ion · ion · chains A
BME · Beta-mercaptoethanol · additive · 2 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1158	0.82	0.83	94	BME, CL, GOL
2	210	0.59	0.81	41	MN, ADP

Modifications

Observed in the structure: 2 covalent (additive adduct).

Compared structures

2JLS · Dengue virus 4 NS3 helicase in complex with ADP · 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 Q2YHF0
Elsewhere: RCSB PDB 2JLS · PDBe 2JLS · UniProt Q2YHF0

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