1HXJ

CRYSTAL STRUCTURE OF THE MAIZE ZM-P60.1 BETA-GLUCOSIDASE

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	0008152	biological_process	metabolic process
A	0008422	molecular_function	beta-glucosidase activity
A	0009507	cellular_component	chloroplast
A	0009536	cellular_component	plastid
A	0009736	biological_process	cytokinin-activated signaling pathway
A	0015923	molecular_function	mannosidase activity
A	0015925	molecular_function	galactosidase activity
A	0015928	molecular_function	fucosidase activity
A	0016162	molecular_function	cellulose 1,4-beta-cellobiosidase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0097599	molecular_function	xylanase activity
A	0102483	molecular_function	scopolin beta-glucosidase activity
A	0102726	molecular_function	DIMBOA glucoside beta-D-glucosidase activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0008152	biological_process	metabolic process
B	0008422	molecular_function	beta-glucosidase activity
B	0009507	cellular_component	chloroplast
B	0009536	cellular_component	plastid
B	0009736	biological_process	cytokinin-activated signaling pathway
B	0015923	molecular_function	mannosidase activity
B	0015925	molecular_function	galactosidase activity
B	0015928	molecular_function	fucosidase activity
B	0016162	molecular_function	cellulose 1,4-beta-cellobiosidase activity
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0097599	molecular_function	xylanase activity
B	0102483	molecular_function	scopolin beta-glucosidase activity
B	0102726	molecular_function	DIMBOA glucoside beta-D-glucosidase activity

Functional Information from PROSITE/UniProt

site_id	PS00572
Number of Residues	9
Details	GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGIG

Chain	Residue	Details
A	ILE397-GLY405

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site_id	PS00653
Number of Residues	15
Details	GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtFGaAtSAYQiEgA

Chain	Residue	Details
A	PHE23-ALA37

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q7XKV4

Chain	Residue	Details
A	GLU186
B	GLU186

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q7XKV4

Chain	Residue	Details
A	GLU401
B	GLU401

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49

Chain	Residue	Details
A	GLN33
B	GLN33

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site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0007744|PDB:1E56

Chain	Residue	Details
A	HIS137
A	ASN185
A	TYR328
A	TYR468
B	HIS137
B	ASN185
B	TYR328
B	TYR468

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site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9

Chain	Residue	Details
B	GLU401
A	GLU401

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site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:11106394, ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49

Chain	Residue	Details
A	TRP452
A	GLU459
B	TRP452
B	GLU459

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