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Influenza virus hemagglutinin

Analyse Influenza virus hemagglutinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VIU
Type: protein
Length: 495 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
UniProt: P03437
Ligands: NAG, BMA
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemagglutinin	protein	320	10% helix, 42% strand	P03437
B	Hemagglutinin	protein	175	53% helix, 15% strand	P03437

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B
BMA · beta-D-mannopyranose · sugar

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

Pockets

4 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	55	0.61	0.92	18	empty
2	75	0.55	0.87	18	empty
3	113	0.36	0.74	18	empty
4	79	0.34	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 2992 Å² buried · 44 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

2VIU · Influenza virus hemagglutinin · 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 P03437
Elsewhere: RCSB PDB 2VIU · PDBe 2VIU · UniProt P03437

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