Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4OEH

X-ray Structure of Uridine Phosphorylase from Vibrio cholerae Complexed with Uracil at 1.91 A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0004850	molecular_function	uridine phosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006152	biological_process	purine nucleoside catabolic process
A	0006218	biological_process	uridine catabolic process
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0009166	biological_process	nucleotide catabolic process
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	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0004850	molecular_function	uridine phosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006152	biological_process	purine nucleoside catabolic process
B	0006218	biological_process	uridine catabolic process
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0009166	biological_process	nucleotide catabolic process
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	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0004850	molecular_function	uridine phosphorylase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006152	biological_process	purine nucleoside catabolic process
C	0006218	biological_process	uridine catabolic process
C	0009116	biological_process	nucleoside metabolic process
C	0009164	biological_process	nucleoside catabolic process
C	0009166	biological_process	nucleotide catabolic process
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	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0004850	molecular_function	uridine phosphorylase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006152	biological_process	purine nucleoside catabolic process
D	0006218	biological_process	uridine catabolic process
D	0009116	biological_process	nucleoside metabolic process
D	0009164	biological_process	nucleoside catabolic process
D	0009166	biological_process	nucleotide catabolic process
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	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0004850	molecular_function	uridine phosphorylase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006152	biological_process	purine nucleoside catabolic process
E	0006218	biological_process	uridine catabolic process
E	0009116	biological_process	nucleoside metabolic process
E	0009164	biological_process	nucleoside catabolic process
E	0009166	biological_process	nucleotide catabolic process
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	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0004850	molecular_function	uridine phosphorylase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006152	biological_process	purine nucleoside catabolic process
F	0006218	biological_process	uridine catabolic process
F	0009116	biological_process	nucleoside metabolic process
F	0009164	biological_process	nucleoside catabolic process
F	0009166	biological_process	nucleotide catabolic process
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	9
Details	BINDING SITE FOR RESIDUE URA A 301

Chain	Residue
A	THR94
A	GLY95
A	PHE161
A	GLN165
A	ARG167
A	GLU195
A	MET196
A	GOL302
A	HOH409

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	THR93
A	MET196
A	GLU197
A	URA301
A	HOH475
A	HOH548
B	HIS7

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	GLN31
A	TYR52
A	HOH431
A	HOH603
A	HOH630

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EOH A 304

Chain	Residue
A	LYS250
A	HOH442

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE URA B 301

Chain	Residue
B	THR93
B	THR94
B	GLY95
B	PHE161
B	GLN165
B	ARG167
B	PHE194
B	GLU195
B	MET196
B	ILE220
B	GOL302
B	HOH411

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 302

Chain	Residue
A	HIS7
B	THR93
B	GLU195
B	MET196
B	GLU197
B	URA301
B	HOH445
B	HOH514

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG B 303

Chain	Residue
B	PHE133
B	THR137
B	LYS140
B	HOH428
B	HOH471
B	HOH480
C	PHE133
C	THR137

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 304

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

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
C	PHE161
C	GLU197
C	HOH427
C	HOH483
C	HOH506
D	HIS7

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 302

Chain	Residue
B	THR110
B	MET152
C	PRO131
C	ASP132
C	PHE133
C	EDO303
C	HOH548

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
C	ASP132
C	ALA206
C	LEU210
C	EDO302
C	HOH413
C	HOH449

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 301

Chain	Residue
C	HIS7
D	PHE161
D	GLU195
D	MET196
D	GLU197
D	HOH566

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 303

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

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE URA E 301

Chain	Residue
E	THR93
E	THR94
E	GLY95
E	PHE161
E	GLN165
E	ARG167
E	GLU195
E	MET196
E	ILE220
E	GOL302
E	HOH404

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 302

Chain	Residue
E	THR93
E	GLU195
E	MET196
E	GLU197
E	URA301
E	HOH411
E	HOH559
F	HIS7

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO E 303

Chain	Residue
E	HIS46
E	ARG47
F	ASP26

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE URA F 301

Chain	Residue
F	GLY95
F	PHE161
F	GLN165
F	ARG167
F	GLU195
F	GOL302
F	HOH428
F	HOH444

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 302

Chain	Residue
E	HIS7
F	THR93
F	GLU195
F	MET196
F	GLU197
F	URA301
F	HOH523

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 303

Chain	Residue
F	ASP132
F	CYS205
F	GLY209
F	LEU210
F	HOH414
F	HOH423

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EOH F 304

Chain	Residue
E	PHE6
F	ARG167

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA F 305

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

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)