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Crystal structure of H5N2 hemagglutinin apo-Q226L mutant from A/CHICKEN/TAIWAN/0502/2012

Analyse Crystal structure of H5N2 hemagglutinin apo-Q226L mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KCJ
Type: protein
Length: 495 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemagglutinin
UniProt: A0A059VBQ9
Ligands: NAG
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemagglutinin	protein	495	23% helix, 30% strand	A0A059VBQ9

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.55	0.77	33	empty
2	52	0.52	0.88	18	empty
3	80	0.31	0.73	19	empty
4	63	0.29	0.74	17	empty

Modifications

Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

6KCJ · Crystal structure of H5N2 hemagglutinin Apo-Q226L mutant from A/chicken/Taiwan/0502/2012 · 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 A0A059VBQ9
Elsewhere: RCSB PDB 6KCJ · PDBe 6KCJ · UniProt A0A059VBQ9

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