Research workbench

Haemagglutinin of 2004 human H3N2 virus

Analyse Haemagglutinin of 2004 human H3N2 virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YP2
Type: protein
Length: 491 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
UniProt: A0FCI1
Ligands: TAM, NAG, MAN
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemagglutinin	protein	491	25% helix, 31% strand	A0FCI1

Ligands and binding sites

TAM · Tris(hydroxyethyl)aminomethane · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A

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

Pockets

3 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	60	0.58	0.90	18	empty
2	126	0.54	0.82	27	empty
3	97	0.37	0.75	17	empty

Modifications

Observed in the structure: 7 glycan, 5 disulfide (N-glycosylation, disulfide).

Compared structures

2YP2 · Haemagglutinin of 2004 Human H3N2 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 A0FCI1
Elsewhere: RCSB PDB 2YP2 · PDBe 2YP2 · UniProt A0FCI1

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