Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EUF

Crystal structure of BAU-bound human uridine phosphorylase 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004850	molecular_function	uridine phosphorylase activity
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006218	biological_process	uridine catabolic process
A	0006220	biological_process	pyrimidine nucleotide metabolic process
A	0006248	biological_process	CMP catabolic process
A	0006249	biological_process	dCMP catabolic process
A	0009032	molecular_function	thymidine phosphorylase activity
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	0042149	biological_process	cellular response to glucose starvation
A	0042802	molecular_function	identical protein binding
A	0044206	biological_process	UMP salvage
A	0046050	biological_process	UMP catabolic process
A	0046074	biological_process	dTMP catabolic process
A	0046079	biological_process	dUMP catabolic process
A	0046108	biological_process	uridine metabolic process
A	0047847	molecular_function	deoxyuridine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004850	molecular_function	uridine phosphorylase activity
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006218	biological_process	uridine catabolic process
B	0006220	biological_process	pyrimidine nucleotide metabolic process
B	0006248	biological_process	CMP catabolic process
B	0006249	biological_process	dCMP catabolic process
B	0009032	molecular_function	thymidine phosphorylase activity
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	0042149	biological_process	cellular response to glucose starvation
B	0042802	molecular_function	identical protein binding
B	0044206	biological_process	UMP salvage
B	0046050	biological_process	UMP catabolic process
B	0046074	biological_process	dTMP catabolic process
B	0046079	biological_process	dUMP catabolic process
B	0046108	biological_process	uridine metabolic process
B	0047847	molecular_function	deoxyuridine phosphorylase activity
C	0003824	molecular_function	catalytic activity
C	0004850	molecular_function	uridine phosphorylase activity
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006218	biological_process	uridine catabolic process
C	0006220	biological_process	pyrimidine nucleotide metabolic process
C	0006248	biological_process	CMP catabolic process
C	0006249	biological_process	dCMP catabolic process
C	0009032	molecular_function	thymidine phosphorylase activity
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	0042149	biological_process	cellular response to glucose starvation
C	0042802	molecular_function	identical protein binding
C	0044206	biological_process	UMP salvage
C	0046050	biological_process	UMP catabolic process
C	0046074	biological_process	dTMP catabolic process
C	0046079	biological_process	dUMP catabolic process
C	0046108	biological_process	uridine metabolic process
C	0047847	molecular_function	deoxyuridine phosphorylase activity
D	0003824	molecular_function	catalytic activity
D	0004850	molecular_function	uridine phosphorylase activity
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006218	biological_process	uridine catabolic process
D	0006220	biological_process	pyrimidine nucleotide metabolic process
D	0006248	biological_process	CMP catabolic process
D	0006249	biological_process	dCMP catabolic process
D	0009032	molecular_function	thymidine phosphorylase activity
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	0042149	biological_process	cellular response to glucose starvation
D	0042802	molecular_function	identical protein binding
D	0044206	biological_process	UMP salvage
D	0046050	biological_process	UMP catabolic process
D	0046074	biological_process	dTMP catabolic process
D	0046079	biological_process	dUMP catabolic process
D	0046108	biological_process	uridine metabolic process
D	0047847	molecular_function	deoxyuridine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BAU A 400

Chain	Residue
A	MET110
A	MET249
A	ASP279
A	ILE281
A	PO4401
A	HOH422
A	HOH453
B	TYR35
B	HIS36
A	THR141
A	SER142
A	GLY143
A	PHE213
A	GLN217
A	ARG219
A	ILE247
A	GLU248

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 401

Chain	Residue
A	GLY60
A	ARG138
A	ILE139
A	GLY140
A	THR141
A	BAU400
A	HOH408
B	ARG94

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BAU B 400

Chain	Residue
A	TYR35
A	HIS36
B	THR141
B	SER142
B	GLY143
B	PHE213
B	GLN217
B	ARG219
B	ILE247
B	GLU248
B	MET249
B	LEU273
B	ILE281
B	PO4401
B	HOH424
B	HOH441

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
A	ARG94
B	GLY60
B	ARG138
B	ILE139
B	GLY140
B	THR141
B	BAU400
B	HOH430
B	HOH485
B	HOH491

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BAU C 400

Chain	Residue
C	MET110
C	THR141
C	SER142
C	GLY143
C	PHE213
C	GLN217
C	ARG219
C	ILE247
C	GLU248
C	MET249
C	LEU273
C	ASP279
C	PO4401
C	HOH443
D	TYR35
D	HIS36

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 401

Chain	Residue
C	GLY60
C	ARG138
C	ILE139
C	GLY140
C	THR141
C	BAU400
C	HOH426
C	HOH435
D	ARG94

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BAU D 400

Chain	Residue
C	TYR35
C	HIS36
D	THR141
D	SER142
D	GLY143
D	PHE213
D	GLN217
D	ARG219
D	ILE247
D	GLU248
D	MET249
D	LEU273
D	ASP279
D	ILE281
D	PO4401
D	HOH414

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 D 401

Chain	Residue
D	HOH435
C	ARG94
D	GLY60
D	ARG138
D	ILE139
D	GLY140
D	THR141
D	BAU400

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER107-LEU122

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:19291308, ECO:0007744\|PDB:3EUF

Chain	Residue	Details
A	GLY60
D	GLY60
D	ARG94
D	ARG138
A	ARG94
A	ARG138
B	GLY60
B	ARG94
B	ARG138
C	GLY60
C	ARG94
C	ARG138

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:20856879, ECO:0007744\|PDB:3EUF, ECO:0007744\|PDB:3NBQ

Chain	Residue	Details
A	SER142
B	SER142
C	SER142
D	SER142

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:19291308, ECO:0000305\|PubMed:20856879, ECO:0007744\|PDB:3EUF, ECO:0007744\|PDB:3NBQ

Chain	Residue	Details
A	GLN217
B	GLN217
C	GLN217
D	GLN217

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
A	GLU121
A	ARG275
A	HIS36

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
B	GLU121
B	ARG275
B	HIS36

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
C	GLU121
C	ARG275
C	HIS36

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1t0u

Chain	Residue	Details
D	GLU121
D	ARG275
D	HIS36

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