1FOB

CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 100K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015926	molecular_function	glucosidase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031218	molecular_function	arabinogalactan endo-1,4-beta-galactosidase activity
A	0045490	biological_process	pectin catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 400

Chain	Residue
A	HOH401
A	HOH402
A	HOH403
A	HOH404
A	HOH405
A	HOH406
A	HOH407

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12484750

Chain	Residue	Details
A	GLU136
A	GLU246
A	ARG45

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 658

Chain	Residue	Details
A	ARG45	electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity, modifies pKa
A	GLU136	activator, increase nucleophilicity, proton acceptor, proton donor
A	GLU246	covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile

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