1FH8

CRYSTAL STRUCTURE OF THE XYLANASE CEX WITH XYLOBIOSE-DERIVED ISOFAGOMINE INHIBITOR

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

Functional Information from PROSITE/UniProt

site_id	PS00591
Number of Residues	11
Details	GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVDVrITELDI

Chain	Residue	Details
A	GLY226-ILE236

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:7918478

Chain	Residue	Details
A	GLU127

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061, ECO:0000269|PubMed:1678739

Chain	Residue	Details
A	GLU233

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1exp

Chain	Residue	Details
A	GLU127
A	GLU233
A	ASP235
A	HIS205

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1exp

Chain	Residue	Details
A	GLU127

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 548

Chain	Residue	Details
A	GLU127	proton acceptor, proton donor
A	ASN169	electrostatic stabiliser
A	HIS205	electrostatic stabiliser
A	GLU233	electrostatic stabiliser, nucleofuge, nucleophile
A	ASP235	electrostatic stabiliser

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