Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PGA

X-ray Structure of the Uridine Phosphorylase From SALMONELLA TYPHIMURIUM in Complex with Inhibitor and Phosphate and Potassium Ion at 1.74 A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004850	molecular_function	uridine phosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0009166	biological_process	nucleotide catabolic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0044206	biological_process	UMP salvage
B	0003824	molecular_function	catalytic activity
B	0004850	molecular_function	uridine phosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0009166	biological_process	nucleotide catabolic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0044206	biological_process	UMP salvage
C	0003824	molecular_function	catalytic activity
C	0004850	molecular_function	uridine phosphorylase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009116	biological_process	nucleoside metabolic process
C	0009164	biological_process	nucleoside catabolic process
C	0009166	biological_process	nucleotide catabolic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0044206	biological_process	UMP salvage
D	0003824	molecular_function	catalytic activity
D	0004850	molecular_function	uridine phosphorylase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009116	biological_process	nucleoside metabolic process
D	0009164	biological_process	nucleoside catabolic process
D	0009166	biological_process	nucleotide catabolic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0044206	biological_process	UMP salvage
E	0003824	molecular_function	catalytic activity
E	0004850	molecular_function	uridine phosphorylase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0009116	biological_process	nucleoside metabolic process
E	0009164	biological_process	nucleoside catabolic process
E	0009166	biological_process	nucleotide catabolic process
E	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0044206	biological_process	UMP salvage
F	0003824	molecular_function	catalytic activity
F	0004850	molecular_function	uridine phosphorylase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009116	biological_process	nucleoside metabolic process
F	0009164	biological_process	nucleoside catabolic process
F	0009166	biological_process	nucleotide catabolic process
F	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0044206	biological_process	UMP salvage

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 7003

Chain	Residue
B	ARG6048
D	GLY3026
D	ARG3030
D	ARG3091
D	ILE3092
D	GLY3093
D	THR3094

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 F 7004

Chain	Residue
F	ARG4091
F	ILE4092
F	GLY4093
F	THR4094
F	HOH7108
A	ARG1048
F	GLY4026

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 7006

Chain	Residue
B	GLY6026
B	ARG6030
B	ARG6091
B	ILE6092
B	GLY6093
B	THR6094
D	ARG3048

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 8001

Chain	Residue
B	GLU6049
B	ILE6069
B	SER6073
D	GLU3049
D	ILE3069
D	SER3073

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 8002

Chain	Residue
A	GLU1049
A	ILE1069
A	SER1073
F	GLU4049
F	ILE4069
F	SER4073

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K E 8221

Chain	Residue
C	GLU2049
C	ILE2069
C	SER2073
E	GLU5049
E	ILE5069
E	SER5073

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ANU D 7013

Chain	Residue
B	HIS6008
B	ARG6048
D	ILE3069
D	THR3094
D	PHE3162
D	GLN3166
D	ARG3168
D	GLU3196
D	MET3197
D	GLU3198
D	HOH7050

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ANU F 7014

Chain	Residue
A	HIS1008
A	ARG1048
F	THR4094
F	PHE4162
F	GLN4166
F	ARG4168
F	GLU4196
F	MET4197
F	GLU4198

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ANU B 7016

Chain	Residue
B	ILE6069
B	THR6094
B	PHE6162
B	GLN6166
B	ARG6168
B	GLU6196
B	MET6197
B	GLU6198
B	HOH8013
B	HOH8071
D	HIS3008
D	ARG3048

Functional Information from PROSITE/UniProt

site_id	PS01232
Number of Residues	16
Details	PNP_UDP_1 Purine and other phosphorylases family 1 signature. StGIGgPStSIaveEL

Chain	Residue	Details
A	SER1066-LEU1081

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
A	ARG1223
A	GLU1080
A	HIS1008

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
B	HIS6008
B	GLU6080
B	ARG6223

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
C	ARG2223
C	GLU2080
C	HIS2008

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
D	GLU3080
D	HIS3008
D	ARG3223

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
E	GLU5080
E	ARG5223
E	HIS5008

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
F	HIS4008
F	GLU4080
F	ARG4223

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)