3LB9

Crystal structure of the B. circulans cpA123 circular permutant

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
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process

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	PRO140-TRP150

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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	MET48-SER59

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10062","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8019418","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 432

Chain	Residue	Details
A	ASN100	modifies pKa
A	TYR134	electrostatic destabiliser
A	GLU143	covalent catalysis, proton shuttle (general acid/base)
A	TYR145	modifies pKa

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 432

Chain	Residue	Details
B	ASN100	modifies pKa
B	TYR134	electrostatic destabiliser
B	GLU143	covalent catalysis, proton shuttle (general acid/base)
B	TYR145	modifies pKa

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site_id	MCSA3
Number of Residues	4
Details	M-CSA 432

Chain	Residue	Details
C	ASN100	modifies pKa
C	TYR134	electrostatic destabiliser
C	GLU143	covalent catalysis, proton shuttle (general acid/base)
C	TYR145	modifies pKa

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