Research workbench

Dengue virus non-structural protein NS1

Analyse Dengue virus non-structural protein NS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OIG
Type: protein
Length: 700 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 1, NS1
UniProt: P17763
Ligands: SO4
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E	Non-structural protein 1, NS1	protein	175	9% helix, 30% strand	P17763

Ligands and binding sites

SO4 · Sulfate ion · ion · 14 copies · chains A, B, E, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	983	0.79	0.80	118	SO4

Interfaces

3 interfaces between chains.

A–B · 909 Å² buried · 18 hydrogen bonds · protein-protein
D–E · 892 Å² buried · 15 hydrogen bonds · protein-protein
A–E · 610 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified, 16 disulfide (engineered, disulfide).

Compared structures

4OIG · Dengue Virus Non-structural Protein NS1 · 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 P17763
Elsewhere: RCSB PDB 4OIG · PDBe 4OIG · UniProt P17763

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