4KTP

Crystal structure of 2-O-alpha-glucosylglycerol phosphorylase in complex with glucose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004555	molecular_function	alpha,alpha-trehalase activity
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0005993	biological_process	trehalose catabolic process
A	0009277	cellular_component	fungal-type cell wall
A	0016757	molecular_function	glycosyltransferase activity
A	0030246	molecular_function	carbohydrate binding
A	0046872	molecular_function	metal ion binding
A	0047402	molecular_function	protein-glucosylgalactosylhydroxylysine glucosidase activity
B	0003824	molecular_function	catalytic activity
B	0004555	molecular_function	alpha,alpha-trehalase activity
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0005993	biological_process	trehalose catabolic process
B	0009277	cellular_component	fungal-type cell wall
B	0016757	molecular_function	glycosyltransferase activity
B	0030246	molecular_function	carbohydrate binding
B	0046872	molecular_function	metal ion binding
B	0047402	molecular_function	protein-glucosylgalactosylhydroxylysine glucosidase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:24828502

Chain	Residue	Details
A	GLU475
B	GLU475

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:24828502, ECO:0007744|PDB:4KTR

Chain	Residue	Details
A	TYR327
B	TYR327

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:24828502, ECO:0007744|PDB:4KTP

Chain	Residue	Details
A	TRP333
A	LYS587
B	TRP333
B	LYS587

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