Research workbench

Structure of fusion glycoprotein from human respiratory syncytial virus

Analyse Structure of fusion glycoprotein from human respiratory syncytial virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OUS
Type: protein
Length: 5,451 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P03420, M1E1E4
Ligands: NAG, BMA, MAN

Structure

x-ray diffraction · 19 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	73	—	P03420
B, D	—	protein	404	—	P03420, M1E1E4
C	—	protein	76	—	P03420
E	—	protein	73	—	P03420
F	—	protein	401	—	P03420, M1E1E4
G	—	protein	76	—	P03420
H	—	protein	395	—	P03420, M1E1E4
I	—	protein	78	—	P03420
J	—	protein	389	—	P03420, M1E1E4
K	—	protein	70	—	P03420
L	—	protein	396	—	P03420, M1E1E4
M	—	protein	225	—	—
N, P, R, T, X	—	protein	213	—	—
O	—	protein	224	—	—
Q	—	protein	229	—	—
S	—	protein	224	—	—
U	—	protein	215	—	—
V	—	protein	209	—	—
W	—	protein	225	—	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains A, N, C, P, E, R, G, T, I, V, K, X, B, F, J, L
BMA · beta-D-mannopyranose · sugar · 6 copies · chains N, P, R, T, V, X
MAN · alpha-D-mannopyranose · sugar · 6 copies · chains N, P, R, T, V, X

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

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 P03420
Every structure of UniProt M1E1E4
Elsewhere: RCSB PDB 6OUS · PDBe 6OUS · UniProt P03420 · UniProt M1E1E4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.