Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RCA

X-ray structure uridine phosphorylase from Vibrio cholerae in complex with 2.2'-anhydrouridine at 1.34 A

Replaces: 5OUR

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	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	0004850	molecular_function	uridine phosphorylase activity
B	0005737	cellular_component	cytoplasm
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	0004850	molecular_function	uridine phosphorylase activity
C	0005737	cellular_component	cytoplasm
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	0004850	molecular_function	uridine phosphorylase activity
D	0005737	cellular_component	cytoplasm
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	0004850	molecular_function	uridine phosphorylase activity
E	0005737	cellular_component	cytoplasm
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	0004850	molecular_function	uridine phosphorylase activity
F	0005737	cellular_component	cytoplasm
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	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	15
Details	binding site for residue BJE A 302

Chain	Residue
A	PHE161
A	GLN165
A	PHE194
A	GLU195
A	MET196
A	GLU197
A	HOH428
A	HOH451
A	HOH535
A	HOH590
B	HIS7
B	ARG47
A	ILE68
A	THR93
A	GLY95

site_id	AC3
Number of Residues	13
Details	binding site for residue BJE B 301

Chain	Residue
A	HIS7
B	ILE68
B	THR93
B	GLY95
B	GLN165
B	PHE194
B	GLU195
B	MET196
B	GLU197
B	HOH462
B	HOH475
B	HOH500
B	HOH553

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL B 302

Chain	Residue
B	LEU115
B	ARG178
B	GLU185
B	HOH401
B	HOH410
B	HOH586
C	PRO124
C	GLU126
D	ARG177

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL B 303

Chain	Residue
B	VAL5
B	PHE6
B	HIS7
B	GLY9
B	HIS46

site_id	AC6
Number of Residues	3
Details	binding site for residue CL C 301

Chain	Residue
C	PHE133
C	HOH564
C	HOH649

site_id	AC7
Number of Residues	12
Details	binding site for residue BJE C 302

Chain	Residue
C	ILE68
C	THR93
C	GLN165
C	GLU195
C	MET196
C	GLU197
C	HOH431
C	HOH449
C	HOH488
C	HOH592
D	HIS7
D	ARG47

site_id	AC8
Number of Residues	6
Details	binding site for residue NA C 303

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

site_id	AC9
Number of Residues	14
Details	binding site for residue BJE D 301

Chain	Residue
C	HIS7
C	ARG47
D	ILE68
D	THR93
D	GLY95
D	GLN165
D	PHE194
D	GLU195
D	MET196
D	GLU197
D	HOH429
D	HOH514
D	HOH538
D	HOH559

site_id	AD1
Number of Residues	11
Details	binding site for residue GOL D 302

Chain	Residue
D	LEU115
D	ARG178
D	PHE179
D	SER182
D	GLU185
D	HOH413
D	HOH434
D	HOH594
E	PRO124
E	GLU126
F	ARG177

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL D 303

Chain	Residue
D	PRO99
D	HIS100
D	ASN102
D	GLN224

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL D 304

Chain	Residue
D	ASP169
D	THR170
D	PHE171
D	HOH454
D	HOH497
C	GLN82

site_id	AD4
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	AD5
Number of Residues	15
Details	binding site for residue BJE E 302

Chain	Residue
E	ILE68
E	THR93
E	GLY95
E	GLN165
E	PHE194
E	GLU195
E	MET196
E	GLU197
E	HOH435
E	HOH505
E	HOH508
E	HOH588
E	HOH639
F	HIS7
F	ARG47

site_id	AD6
Number of Residues	6
Details	binding site for residue MG E 303

Chain	Residue
B	HOH664
E	HOH640
E	HOH710
E	HOH716
F	HOH648
F	HOH719

site_id	AD7
Number of Residues	14
Details	binding site for residue BJE F 301

Chain	Residue
E	HIS7
E	ARG47
F	ILE68
F	THR93
F	GLY95
F	GLN165
F	PHE194
F	GLU195
F	MET196
F	GLU197
F	HOH427
F	HOH488
F	HOH495
F	HOH609

site_id	AD8
Number of Residues	4
Details	binding site for residue EDO F 302

Chain	Residue
A	MET125
F	MET125
F	HOH656
F	HOH672

site_id	AD9
Number of Residues	12
Details	binding site for residue GOL F 303

Chain	Residue
A	PRO124
A	GLU126
B	ARG177
F	LEU115
F	ARG178
F	PHE179
F	SER182
F	GLU185
F	TRP186
F	HOH404
F	HOH437
F	HOH523

site_id	AE1
Number of Residues	9
Details	binding site for residue GOL F 304

Chain	Residue
A	ILE227
A	ASP229
A	HOH648
A	HOH665
A	HOH712
F	LYS184
F	GLN187
F	ASP188
F	HOH424

site_id	AE2
Number of Residues	5
Details	binding site for residue GOL F 305

Chain	Residue
E	ASP169
E	PHE171
F	GLN82
F	HOH454
F	HOH575

site_id	AE3
Number of Residues	2
Details	binding site for residue CL F 306

Chain	Residue
F	PHE133
F	HOH547

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)