7FE3

Crystal structure of GH65 alpha-1,2-glucosidase from Flavobacterium johnsoniae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0016757	molecular_function	glycosyltransferase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030246	molecular_function	carbohydrate binding
A	0042597	cellular_component	periplasmic space
B	0003824	molecular_function	catalytic activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0016757	molecular_function	glycosyltransferase activity
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0030246	molecular_function	carbohydrate binding
B	0042597	cellular_component	periplasmic space
C	0003824	molecular_function	catalytic activity
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0016757	molecular_function	glycosyltransferase activity
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0030246	molecular_function	carbohydrate binding
C	0042597	cellular_component	periplasmic space

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:34728215, ECO:0000305\|PubMed:37269952

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:34728215, ECO:0000305\|PubMed:37269952

site_id	SWS_FT_FI3
Number of Residues	33
Details	BINDING: BINDING => ECO:0000269\|PubMed:34728215, ECO:0007744\|PDB:7FE4