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Structure of human respiratory syncytial virus non-structural protein 1 (NS1)

Analyse Structure of human respiratory syncytial virus non-structural protein 1 (NS1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VJ2
Type: protein
Length: 270 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 1
UniProt: X5FN71
Ligands: CL
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Non-structural protein 1	protein	135	21% helix, 48% strand	X5FN71

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A, B
DIO · 1,4-diethylene dioxide · additive · 5 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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	677	0.84	0.88	81	DIO, CL, GOL

Interfaces

1 interface between chains.

A–B · 1015 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5VJ2 · Structure of human respiratory syncytial virus non-structural protein 1 (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 X5FN71
Elsewhere: RCSB PDB 5VJ2 · PDBe 5VJ2 · UniProt X5FN71

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