Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4R31

Crystal structure of a putative uridine phosphorylase from Actinobacillus succinogenes 130Z (Target NYSGRC-029667 )

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	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0044206	biological_process	UMP salvage
A	0047847	molecular_function	deoxyuridine phosphorylase activity
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	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0044206	biological_process	UMP salvage
B	0047847	molecular_function	deoxyuridine phosphorylase activity
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	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0044206	biological_process	UMP salvage
C	0047847	molecular_function	deoxyuridine phosphorylase activity
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	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0044206	biological_process	UMP salvage
D	0047847	molecular_function	deoxyuridine phosphorylase activity
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	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0044206	biological_process	UMP salvage
E	0047847	molecular_function	deoxyuridine phosphorylase activity
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	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0044206	biological_process	UMP salvage
F	0047847	molecular_function	deoxyuridine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	PHE160
A	MSE195
A	GLU196
D	HIS6

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	PRO176
A	ALA177
A	GLN179
A	HOH442
E	PRO176

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

Chain	Residue
B	GLU196
F	HIS6

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 302

Chain	Residue
B	VAL129
B	ALA130
B	PHE132
D	THR109
D	ALA130
D	PHE132

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
A	ALA130
A	ASP131
A	THR135
C	THR109
C	VAL129
C	ALA130
C	PHE132

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 302

Chain	Residue
C	GLU196
E	HIS6

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 303

Chain	Residue
C	THR93
C	GLY94
C	PHE160
C	GLN164
C	ARG166
C	TYR193

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 301

Chain	Residue
A	HIS6
A	ARG46
D	PHE160
D	MSE195
D	GLU196
D	HOH468
D	HOH520

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL E 301

Chain	Residue
C	HIS6
E	PHE160
E	MSE195
E	GLU196

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E 302

Chain	Residue
E	ALA130
E	ASP131
E	PHE132
E	THR135
F	THR109
F	VAL129
F	ALA130
F	PHE132

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL F 301

Chain	Residue
B	HIS6
F	GLU196
F	HOH544

Functional Information from PROSITE/UniProt

site_id	PS01232
Number of Residues	16
Details	PNP_UDP_1 Purine and other phosphorylases family 1 signature. StGIGgPSvSIcveEL

Chain	Residue	Details
A	SER64-LEU79

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