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The crystal structure of hemagglutinin from influenza virus A/VICTORIA/361/2011 in complex with 3'SLN

Analyse The crystal structure of hemagglutinin from influenza virus A/VICTORIA/361/2011… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WE9
Type: protein
Length: 491 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
UniProt: R9U684
Ligands: NAG
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemagglutinin	protein	491	24% helix, 32% strand	R9U684

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A

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

Pockets

5 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	56	0.59	0.91	17	empty
2	56	0.58	0.91	17	empty
3	143	0.40	0.74	22	empty
4	77	0.39	0.78	15	empty
5	55	0.28	0.74	15	empty

Modifications

Observed in the structure: 8 glycan, 6 disulfide (N-glycosylation, disulfide).

Compared structures

4WE9 · The crystal structure of hemagglutinin from influenza virus A/Victoria/361/2011 in… · 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 R9U684
Elsewhere: RCSB PDB 4WE9 · PDBe 4WE9 · UniProt R9U684

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