5IHR

STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN COMPLEX WITH ALLOLACTOSE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process

Functional Information from PROSITE/UniProt

site_id	PS01182
Number of Residues	13
Details	GLYCOSYL_HYDROL_F35 Glycosyl hydrolases family 35 putative active site. GGPIIlyQpENEY

Chain	Residue	Details
A	GLY189-TYR201

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:28391618

Chain	Residue	Details
A	GLU200

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:28391618

Chain	Residue	Details
A	GLN298

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5JUV

Chain	Residue	Details
A	TYR96
A	ASN140
A	ASN199
A	TYR364

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site_id	SWS_FT_FI4
Number of Residues	9
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP

Chain	Residue	Details
A	ASN156
A	ASN402
A	ASN478
A	ASN522
A	ASN622
A	ASN739
A	ASN760
A	ASN777
A	ASN914

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN422
A	ASN805

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