2F24

Crystal Structure of the Human Sialidase Neu2 E111Q Mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004308	molecular_function	exo-alpha-sialidase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005829	cellular_component	cytosol
A	0006516	biological_process	glycoprotein catabolic process
A	0006689	biological_process	ganglioside catabolic process
A	0009313	biological_process	oligosaccharide catabolic process
A	0016020	cellular_component	membrane
A	0016042	biological_process	lipid catabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046479	biological_process	glycosphingolipid catabolic process
A	0052794	molecular_function	exo-alpha-(2->3)-sialidase activity
A	0052795	molecular_function	exo-alpha-(2->6)-sialidase activity
A	0052796	molecular_function	exo-alpha-(2->8)-sialidase activity
A	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1001

Chain	Residue
A	LEU28
A	GLY30
A	GLN31
A	HOH1060

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:22228546

Chain	Residue	Details
A	ASP46

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
A	TYR334

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
A	GLU355

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site_id	SWS_FT_FI4
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
A	ARG21
A	ARG41
A	TYR179
A	TYR181
A	GLU218
A	ARG237
A	ARG304

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