1DEO

RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10801485","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"10801485","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10801485","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11752785","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18645234","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"10801485","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11752785","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18645234","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 705

Chain	Residue	Details
A	SER9	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLY42	electrostatic stabiliser
A	ASN74	electrostatic stabiliser
A	ASP192	electrostatic stabiliser, increase basicity
A	HIS195	proton acceptor, proton donor

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