Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4IP0

X-Ray Structure of the Complex Uridine Phosphorylase from Vibrio cholerae with Phosphate Ion at 1.29 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
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	4
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
C	GLN31
A	HOH578
A	HOH670
A	HOH747

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 301

Chain	Residue
B	ARG86
B	HOH516

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 302

Chain	Residue
A	ARG47
B	GLY25
B	ARG29
B	ARG90
B	VAL91
B	GLY92
B	THR93
B	HOH439
B	HOH489

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 303

Chain	Residue
B	LYS140
B	GLN144
B	HOH604
B	HOH626
B	HOH655

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 304

Chain	Residue
B	ARG177
B	HOH457
B	HOH505
D	ARG177
F	ARG177

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 305

Chain	Residue
A	GLY92
A	THR93
A	HOH550
A	HOH564
B	ARG47
B	HOH634

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EOH B 306

Chain	Residue
B	HOH413
B	HOH437
B	HOH438

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 C 301

Chain	Residue
C	GLY25
C	ARG29
C	ARG90
C	VAL91
C	GLY92
C	THR93
C	HOH442
C	HOH573
C	HOH581
D	ARG47

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 302

Chain	Residue
C	GLY95
C	ARG167
C	ILE220
C	EDO303

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
C	THR94
C	GLY95
C	PHE161
C	GLN165
C	PHE194
C	GLU195
C	MET196
C	CL302
C	HOH524
C	HOH573
C	HOH579
C	HOH580

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 304

Chain	Residue
C	ARG239
C	LYS242
C	HOH703

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 301

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

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 302

Chain	Residue
C	HOH458
C	HOH517
D	HIS46
D	HOH443
D	HOH533
D	HOH586
D	HOH676

site_id	BC6
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	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 E 302

Chain	Residue
E	ARG90
E	GLY92
E	THR93
E	HOH441
E	HOH581
E	HOH627
E	HOH731
F	ARG47

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 303

Chain	Residue
E	ARG86
E	HOH663
E	HOH687

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO E 304

Chain	Residue
E	GLU166
E	MET183
E	ARG222
E	HOH693
E	HOH706

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 F 301

Chain	Residue
E	ARG47
F	GLY25
F	ARG29
F	ARG90
F	VAL91
F	GLY92
F	THR93
F	HOH467
F	HOH575
F	HOH585

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 F 302

Chain	Residue
F	LYS140
F	GLN144
F	HOH520
F	HOH523
F	HOH527
F	HOH588
F	HOH643
F	HOH658

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL F 303

Chain	Residue
F	GLY95
F	ARG167
F	ILE220
F	EDO304

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EDO F 304

Chain	Residue
F	THR94
F	GLY95
F	GLN165
F	PHE194
F	GLU195
F	MET196
F	CL303
F	HOH575
F	HOH577
F	HOH578
F	HOH579
F	HOH585

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO F 305

Chain	Residue
A	SER207
A	SER208
A	GLY209
B	ARG174
F	ASP188
F	MET189
F	GLY190
F	HOH425
F	HOH716

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)