Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5EFO

X-ray structure uridine phosphorylase from Vibrio cholerae in complex with cytidine and cytosine at 1.63A.

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
A	0046872	molecular_function	metal ion binding
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
B	0046872	molecular_function	metal ion binding
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
C	0046872	molecular_function	metal ion binding
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
D	0046872	molecular_function	metal ion binding
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
E	0046872	molecular_function	metal ion binding
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
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue NA A 301

Chain	Residue
A	GLU48
A	ILE68
A	SER72
B	GLU48
B	ILE68
B	SER72

site_id	AC2
Number of Residues	9
Details	binding site for residue CYT A 302

Chain	Residue
A	ARG167
A	GLU195
A	MET196
A	TRS303
A	HOH413
A	HOH492
A	GLY95
A	PHE161
A	GLN165

site_id	AC3
Number of Residues	10
Details	binding site for residue TRS A 303

Chain	Residue
A	ILE68
A	GLU195
A	MET196
A	GLU197
A	CYT302
A	HOH418
A	HOH424
A	HOH497
B	HIS7
B	ARG47

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL B 301

Chain	Residue
A	HIS7
B	THR93
B	PHE161
B	GLU195
B	MET196
B	GLU197
B	CYT302
B	HOH416
B	HOH482

site_id	AC5
Number of Residues	9
Details	binding site for residue CYT B 302

Chain	Residue
B	THR94
B	GLY95
B	PHE161
B	GLN165
B	ARG167
B	GLU195
B	MET196
B	GOL301
B	HOH445

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL C 301

Chain	Residue
C	ILE68
C	GLU195
C	MET196
C	GLU197
C	CYT303
C	HOH449
C	HOH455
D	HIS7

site_id	AC7
Number of Residues	5
Details	binding site for residue PEG C 302

Chain	Residue
C	GLN98
C	GLN187
C	ASP188
C	HOH414
C	HOH459

site_id	AC8
Number of Residues	10
Details	binding site for residue CYT C 303

Chain	Residue
C	PHE161
C	GLN165
C	ARG167
C	GLU195
C	MET196
C	ARG222
C	GOL301
C	HOH401
C	HOH402
C	HOH407

site_id	AC9
Number of Residues	8
Details	binding site for residue CYT C 304

Chain	Residue
B	GLU126
C	ARG178
C	PHE179
C	SER182
C	GLU185
C	TRP186
C	HOH425
C	HOH542

site_id	AD1
Number of Residues	6
Details	binding site for residue NA C 305

Chain	Residue
C	GLU48
C	ILE68
C	SER72
D	GLU48
D	ILE68
D	SER72

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO D 301

Chain	Residue
D	ARG167
D	TYR168
D	ASP169
D	HOH415
D	HOH427

site_id	AD3
Number of Residues	9
Details	binding site for residue CYT D 302

Chain	Residue
D	GLY95
D	PHE161
D	GLN165
D	ARG167
D	GLU195
D	MET196
D	ILE220
D	GOL304
D	HOH430

site_id	AD4
Number of Residues	10
Details	binding site for residue CYT D 303

Chain	Residue
D	HOH406
D	HOH482
D	HOH578
E	GLU126
F	ARG177
D	ARG178
D	PHE179
D	GLU185
D	TRP186
D	HOH402

site_id	AD5
Number of Residues	8
Details	binding site for residue GOL D 304

Chain	Residue
C	HIS7
D	ILE68
D	GLU195
D	MET196
D	GLU197
D	CYT302
D	HOH458
D	HOH522

site_id	AD6
Number of Residues	6
Details	binding site for residue NA E 301

Chain	Residue
E	GLU48
E	ILE68
E	SER72
F	GLU48
F	ILE68
F	SER72

site_id	AD7
Number of Residues	12
Details	binding site for residue GOL E 302

Chain	Residue
E	PRO24
E	GLY25
E	ASP26
E	ARG29
E	ARG90
E	VAL91
E	GLY92
E	THR93
E	CTN303
E	HOH412
E	HOH512
F	ARG47

site_id	AD8
Number of Residues	17
Details	binding site for residue CTN E 303

Chain	Residue
E	THR93
E	THR94
E	GLY95
E	PHE161
E	GLN165
E	ARG167
E	PHE194
E	GLU195
E	MET196
E	GLU197
E	ILE220
E	GOL302
E	HOH412
E	HOH476
E	HOH496
E	HOH512
F	HIS7

site_id	AD9
Number of Residues	3
Details	binding site for residue EDO F 301

Chain	Residue
E	PHE6
F	ARG167
F	ASP169

site_id	AE1
Number of Residues	7
Details	binding site for residue EDO F 302

Chain	Residue
A	HOH415
E	LEU120
F	ARG178
F	HOH401
F	HOH428
F	HOH439
F	HOH593

site_id	AE2
Number of Residues	14
Details	binding site for residue CTN F 303

Chain	Residue
E	HIS7
F	THR93
F	THR94
F	GLY95
F	PHE161
F	GLN165
F	ARG167
F	GLU195
F	MET196
F	GLU197
F	ILE220
F	HOH409
F	HOH521
F	HOH537

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	SER65-LEU80

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