MolNFT v1 · #108673 · protein

Structure and receptor binding prefereneces of recombinant human A(H3N2) virus hemagglutinins

4WEA: “Structure and receptor binding prefereneces of recombinant human A(H3N2) virus hemagglutinins”. X-ray diffraction, 2 ligands (NAG, SIA), 4 pockets (best druggability 0.59). MolNFT v1 #108673 on GenesisL1: 3D structure, binding sites…

PDB: 4WEA
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, SIA
Pockets: 4 · 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
SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A

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

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.59	0.92	17	empty
2	156	0.41	0.74	27	empty
3	68	0.36	0.77	15	empty
4	82	0.33	0.74	17	SIA

Modifications

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

Compared structures

4WEA · Structure and receptor binding prefereneces of recombinant human A(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 R9U684
Elsewhere: RCSB PDB 4WEA · PDBe 4WEA · UniProt R9U684

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