1BYH

MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE

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
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0042972	molecular_function	licheninase activity

Functional Information from PROSITE/UniProt

site_id	PS01034
Number of Residues	11
Details	GH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT

Chain	Residue	Details
A	GLU105-THR115

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	209
Details	Domain: {"description":"GH16","evidences":[{"source":"PROSITE-ProRule","id":"PRU01098","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10064","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10064","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 2ayh

Chain	Residue	Details
A	GLU109
A	ASP107
A	GLU105

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 924

Chain	Residue	Details
A	GLU105	covalent catalysis
A	GLU109	proton shuttle (general acid/base)

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