2ICY

Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UDP-glucose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005977	biological_process	glycogen metabolic process
A	0005985	biological_process	sucrose metabolic process
A	0006011	biological_process	UDP-glucose metabolic process
A	0009555	biological_process	pollen development
A	0016036	biological_process	cellular response to phosphate starvation
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0052543	biological_process	callose deposition in cell wall
A	0070569	molecular_function	uridylyltransferase activity
A	0090406	cellular_component	pollen tube
B	0003983	molecular_function	UTP:glucose-1-phosphate uridylyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005977	biological_process	glycogen metabolic process
B	0005985	biological_process	sucrose metabolic process
B	0006011	biological_process	UDP-glucose metabolic process
B	0009555	biological_process	pollen development
B	0016036	biological_process	cellular response to phosphate starvation
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0052543	biological_process	callose deposition in cell wall
B	0070569	molecular_function	uridylyltransferase activity
B	0090406	cellular_component	pollen tube

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS A 900

Chain	Residue
A	ILE157
A	HIS158
A	THR159
A	LYS204

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site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE UPG A 901

Chain	Residue
A	PRO189
A	GLY191
A	HIS192
A	ASN220
A	SER221
A	ASN293
A	THR294
A	ASN295
A	PHE356
A	HOH927
A	HOH962
A	HOH1049
A	HOH1138
A	HOH1192
A	LEU85
A	GLY87
A	GLY88
A	MET134
A	GLN162

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HOH B 903

Chain	Residue
B	ALA14
B	LEU18
B	SER178

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:17178129, ECO:0007744|PDB:2ICX

Chain	Residue	Details
A	LEU85
B	GLY191
B	ASP222
B	LYS360
A	LYS99
A	GLN162
A	GLY191
A	ASP222
A	LYS360
B	LEU85
B	LYS99
B	GLN162

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q16851

Chain	Residue	Details
A	GLY87
A	HIS192
A	ASN220
B	GLY87
B	HIS192
B	ASN220

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895

Chain	Residue	Details
A	ALA2
B	ALA2

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