1LL7

STRUCTURE OF THE E171Q MUTANT OF C. IMMITIS CHITINASE 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004568	molecular_function	chitinase activity
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0006032	biological_process	chitin catabolic process
A	0008061	molecular_function	chitin binding
A	0008843	molecular_function	endochitinase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0000272	biological_process	polysaccharide catabolic process
B	0004568	molecular_function	chitinase activity
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0006032	biological_process	chitin catabolic process
B	0008061	molecular_function	chitin binding
B	0008843	molecular_function	endochitinase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258

Chain	Residue	Details
A	GLN171
B	GLN171

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site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258

Chain	Residue	Details
A	GLY102
B	TRP378
A	GLY129
A	TYR172
A	MET237
A	TRP378
B	GLY102
B	GLY129
B	TYR172
B	MET237

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	ASP169
B	ASP169

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN387
B	ASN387

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