1C5H

HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE

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	0031176	molecular_function	endo-1,4-beta-xylanase activity
A	0045493	biological_process	xylan catabolic process

Functional Information from PDB Data

site_id	ABC
Number of Residues	1
Details	THE ACID BASE CATALYST IS RESIDUE GLU 172.

Chain	Residue
A	GLU172

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site_id	NUC
Number of Residues	1
Details	THE NUCLEOPHILE IS RESIDUE GLU 78.

Chain	Residue
A	GLU78

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Functional Information from PROSITE/UniProt

site_id	PS00776
Number of Residues	11
Details	GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW

Chain	Residue	Details
A	PRO75-TRP85

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site_id	PS00777
Number of Residues	12
Details	GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS

Chain	Residue	Details
A	MET169-SER180

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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:PRU10062, ECO:0000269|PubMed:8019418

Chain	Residue	Details
A	GLU78

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418

Chain	Residue	Details
A	GLU172

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1bvv

Chain	Residue	Details
A	GLU172
A	GLU78

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 432

Chain	Residue	Details
A	ASP35	modifies pKa
A	TYR69	electrostatic destabiliser
A	GLU78	covalent catalysis, proton shuttle (general acid/base)
A	TYR80	modifies pKa
A	GLU172	proton shuttle (general acid/base)

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