1GLH

CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 330

Chain	Residue
A	PRO9
A	GLY45
A	TYR56
A	ASP207

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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	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10064

Chain	Residue	Details
A	GLU105

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10064

Chain	Residue	Details
A	GLU109

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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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