1NP0

Human lysosomal beta-hexosaminidase isoform B in complex with intermediate analogue NAG-thiazoline

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004563	molecular_function	beta-N-acetylhexosaminidase activity
C	0005975	biological_process	carbohydrate metabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004563	molecular_function	beta-N-acetylhexosaminidase activity
D	0005975	biological_process	carbohydrate metabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0004563	molecular_function	beta-N-acetylhexosaminidase activity
E	0005975	biological_process	carbohydrate metabolic process
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0004563	molecular_function	beta-N-acetylhexosaminidase activity
F	0005975	biological_process	carbohydrate metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:11329289

Chain	Residue	Details
D	GLU355
F	GLU355
E	ASN142
E	ASN190

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Not glycosylated => ECO:0000269|PubMed:11447134

Chain	Residue	Details
D	ASN497
F	ASN497

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11447134, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218

Chain	Residue	Details
D	ASN327
F	ASN327

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
A	ASP354
A	GLU355

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
B	ASP354
B	GLU355

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