3H55

Crystal Structure of human alpha-N-acetylgalactosaminidase, Complex with Galactose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004557	molecular_function	alpha-galactosidase activity
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005975	biological_process	carbohydrate metabolic process
A	0006629	biological_process	lipid metabolic process
A	0008152	biological_process	metabolic process
A	0008456	molecular_function	alpha-N-acetylgalactosaminidase activity
A	0009311	biological_process	oligosaccharide metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016139	biological_process	glycoside catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0019377	biological_process	glycolipid catabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0070062	cellular_component	extracellular exosome
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004557	molecular_function	alpha-galactosidase activity
B	0005737	cellular_component	cytoplasm
B	0005764	cellular_component	lysosome
B	0005975	biological_process	carbohydrate metabolic process
B	0006629	biological_process	lipid metabolic process
B	0008152	biological_process	metabolic process
B	0008456	molecular_function	alpha-N-acetylgalactosaminidase activity
B	0009311	biological_process	oligosaccharide metabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016139	biological_process	glycoside catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0019377	biological_process	glycolipid catabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00512
Number of Residues	16
Details	ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GYtyLnIDDc.Wigg....RD

Chain	Residue	Details
A	GLY71-ASP86

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile

Chain	Residue	Details
A	ASP156
B	ASP156

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	ASP217
B	ASP217

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site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING:

Chain	Residue	Details
A	ASP78
B	ASP217
A	LYS154
A	SER188
A	ARG213
A	ASP217
B	ASP78
B	LYS154
B	SER188
B	ARG213

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17693683

Chain	Residue	Details
A	SER322
A	SER332
B	SER322
B	SER332

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site_id	SWS_FT_FI5
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19683538

Chain	Residue	Details
A	ASN124
A	ASN385
B	ASN124
B	ASN385

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site_id	SWS_FT_FI6
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19683538

Chain	Residue	Details
A	ASN177
B	ASN177

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site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	GLN201
B	GLN201

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN359
B	ASN359

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