Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4OGL

X-ray structure uridine phosphorylase from Vibrio cholerae in complex with thymine at 1.25 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	12
Details	BINDING SITE FOR RESIDUE TDR A 301

Chain	Residue
A	THR93
A	ILE220
A	GOL303
A	HOH402
A	THR94
A	GLY95
A	PHE161
A	GLN165
A	ARG167
A	GLU195
A	MET196
A	ILE219

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
A	ARG178
A	HOH408
A	HOH409
A	HOH603
A	HOH674
A	HOH721
B	LEU120
F	HOH626

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 303

Chain	Residue
A	GLU197
A	TDR301
A	HOH459
A	HOH503
A	HOH527
A	HOH723
B	HIS7

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 304

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

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TDR B 301

Chain	Residue
B	GLY95
B	PHE161
B	GLN165
B	ARG167
B	GLU195
B	MET196
B	ILE220
B	TRS303
B	HOH418
B	HOH732

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 302

Chain	Residue
B	PHE6
B	HIS7
B	GLY9
B	HIS46
B	HOH711

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS B 303

Chain	Residue
A	HIS7
A	ARG47
B	ILE68
B	THR93
B	GLU195
B	MET196
B	GLU197
B	TDR301
B	HOH467
B	HOH509

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TDR C 301

Chain	Residue
C	THR94
C	GLY95
C	PHE161
C	GLN165
C	ARG167
C	PHE194
C	GLU195
C	MET196
C	ILE220
C	GOL305
C	HOH408

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 302

Chain	Residue
B	HOH724
C	ARG178
C	HOH414
C	HOH417
C	HOH643
C	HOH649
C	HOH683
D	LEU120

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
C	ASP132
C	HOH407
C	HOH426
C	HOH554
C	HOH766

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 304

Chain	Residue
C	LYS3
C	GLN82
C	HOH674
D	ASP169
D	THR170
D	PHE171
D	HOH544

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 305

Chain	Residue
C	PHE161
C	GLU197
C	TDR301
C	HOH476
C	HOH491
D	HIS7

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 306

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

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TDR D 301

Chain	Residue
D	THR94
D	GLY95
D	PHE161
D	GLN165
D	ARG167
D	GLU195
D	MET196
D	ILE220
D	GOL302
D	HOH409

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 302

Chain	Residue
C	HIS7
C	ARG47
D	ILE68
D	PHE161
D	GLU197
D	TDR301
D	GOL303
D	HOH452
D	HOH468

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 303

Chain	Residue
C	ARG47
C	HOH791
D	PHE161
D	GLU226
D	GOL302

site_id	BC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TDR E 301

Chain	Residue
E	GLY95
E	PHE161
E	GLN165
E	ARG167
E	GLU195
E	MET196
E	ILE220
E	GOL304
E	HOH421
E	HOH485
E	HOH545
E	HOH742

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO E 302

Chain	Residue
C	HOH501
D	MET125
E	MET125
E	HOH744

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO E 303

Chain	Residue
E	ARG178
E	HOH407
E	HOH420
E	HOH581
E	HOH598
E	HOH664
E	HOH745
F	LEU120

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL E 304

Chain	Residue
E	ILE68
E	THR93
E	PHE161
E	MET196
E	GLU197
E	TDR301
E	HOH453
E	HOH655
F	HIS7
F	HOH646

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

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

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TDR F 301

Chain	Residue
F	THR93
F	THR94
F	GLY95
F	PHE161
F	GLN165
F	ARG167
F	GLU195
F	MET196
F	ILE219
F	ILE220
F	GOL304
F	HOH406

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO F 302

Chain	Residue
F	GLY17
F	GLN59
F	SER60
F	HOH461

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO F 303

Chain	Residue
A	MET125
A	HOH461
E	HOH493
F	MET125

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 304

Chain	Residue
E	HIS7
F	PHE161
F	GLU197
F	TDR301
F	HOH468
F	HOH470
F	HOH557

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)