Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JLR

STRUCTURE OF THE URACIL PHOSPHORIBOSYLTRANSFERASE GTP COMPLEX 2 MUTANT C128V

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004845	molecular_function	uracil phosphoribosyltransferase activity
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0016757	molecular_function	glycosyltransferase activity
A	0044206	biological_process	UMP salvage
B	0004845	molecular_function	uracil phosphoribosyltransferase activity
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0016757	molecular_function	glycosyltransferase activity
B	0044206	biological_process	UMP salvage
C	0004845	molecular_function	uracil phosphoribosyltransferase activity
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0016757	molecular_function	glycosyltransferase activity
C	0044206	biological_process	UMP salvage
D	0004845	molecular_function	uracil phosphoribosyltransferase activity
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0016757	molecular_function	glycosyltransferase activity
D	0044206	biological_process	UMP salvage

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 799

Chain	Residue
D	ARG112
D	ALA113
D	ASP235
D	GLY237

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 800

Chain	Residue
B	ARG112
B	ALA113
B	ASP235

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 801

Chain	Residue
D	THR169
D	ALA170
D	GLY171
D	SER172
D	HOH825
D	ARG137
D	ALA168

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 C 802

Chain	Residue
C	ARG112
C	ALA113
C	ASP235

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 803

Chain	Residue
C	ARG137
C	ALA168
C	THR169
C	ALA170
C	GLY171
C	SER172
C	HOH815

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 804

Chain	Residue
B	ALA168
B	THR169
B	ALA170
B	GLY171
B	SER172
B	HOH830

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 805

Chain	Residue
A	VAL111
A	ARG112
A	ALA113
A	ASP235
A	HOH843
D	TYR148
D	LYS150

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 806

Chain	Residue
A	ARG137
A	ALA168
A	THR169
A	ALA170
A	GLY171
A	SER172
A	HOH809

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GTP C 300

Chain	Residue
A	GLN44
A	TYR65
A	ARG68
B	LYS59
C	LEU78
C	LEU81
C	PHE101
C	TYR102
C	SER103
C	ILE105
C	ARG129
C	ARG158

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GTP B 301

Chain	Residue
B	LEU78
B	LEU81
B	PHE101
B	TYR102
B	SER103
B	LYS104
B	ILE105
B	ARG129
B	ARG158
B	HOH805
C	LYS59
D	GLN44
D	TYR65
D	ARG68
D	HOH833

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GTP D 302

Chain	Residue
A	LYS59
B	GLN44
B	TYR65
B	ARG68
D	LEU78
D	LEU81
D	PHE101
D	TYR102
D	SER103
D	LYS104
D	ILE105
D	ARG129
D	ARG158
D	HOH804

site_id	BC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GTP A 303

Chain	Residue
A	LEU78
A	PHE101
A	LYS104
A	CYS125
A	ARG129
A	ARG158
A	HOH807
A	HOH814
A	HOH841
C	GLN44
C	TYR65
C	ARG68
C	HOH828
D	LYS59

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:9628859, ECO:0007744\|PDB:1BD3, ECO:0007744\|PDB:1UPU

Chain	Residue	Details
A	LYS59
B	LYS59
D	LYS59
C	LYS59

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:11773618, ECO:0007744\|PDB:1JLR

Chain	Residue	Details
A	ARG68
A	TYR102
B	ARG68
B	TYR102
D	ARG68
D	TYR102
C	ARG68
C	TYR102

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:11773618, ECO:0007744\|PDB:1JLS

Chain	Residue	Details
A	ARG112
B	ARG112
D	ARG112
C	ARG112

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11773618, ECO:0000269\|PubMed:9628859, ECO:0007744\|PDB:1BD3, ECO:0007744\|PDB:1BD4, ECO:0007744\|PDB:1JLR, ECO:0007744\|PDB:1JLS, ECO:0007744\|PDB:1UPU

Chain	Residue	Details
A	ARG129
C	ARG129
C	ARG137
C	ARG158
A	ARG137
A	ARG158
B	ARG129
B	ARG137
B	ARG158
D	ARG129
D	ARG137
D	ARG158

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:11773618, ECO:0000269\|PubMed:9628859, ECO:0007744\|PDB:1JLS, ECO:0007744\|PDB:1UPU

Chain	Residue	Details
A	ASP164
B	ASP164
D	ASP164
C	ASP164

site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:9628859, ECO:0007744\|PDB:1UPU

Chain	Residue	Details
A	ILE229
A	GLY234
B	ILE229
B	GLY234
D	ILE229
D	GLY234
C	ILE229
C	GLY234

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:11773618, ECO:0007744\|PDB:1JLR, ECO:0007744\|PDB:1JLS

Chain	Residue	Details
A	ASP235
B	ASP235
D	ASP235
C	ASP235

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd3

Chain	Residue	Details
A	THR141
A	ARG137
A	ASP235

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd3

Chain	Residue	Details
B	THR141
B	ARG137
B	ASP235

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd3

Chain	Residue	Details
D	THR141
D	ARG137
D	ASP235

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1bd3

Chain	Residue	Details
C	THR141
C	ARG137
C	ASP235

site_id	MCSA1
Number of Residues	4
Details	M-CSA 420

Chain	Residue	Details
A	ARG137	electrostatic stabiliser
A	THR141	electrostatic stabiliser
A	ASP235	electrostatic stabiliser
A	ASP238	modifies pKa

site_id	MCSA2
Number of Residues	4
Details	M-CSA 420

Chain	Residue	Details
B	ARG137	electrostatic stabiliser
B	THR141	electrostatic stabiliser
B	ASP235	electrostatic stabiliser
B	ASP238	modifies pKa

site_id	MCSA3
Number of Residues	4
Details	M-CSA 420

Chain	Residue	Details
D	ARG137	electrostatic stabiliser
D	THR141	electrostatic stabiliser
D	ASP235	electrostatic stabiliser
D	ASP238	modifies pKa

site_id	MCSA4
Number of Residues	4
Details	M-CSA 420

Chain	Residue	Details
C	ARG137	electrostatic stabiliser
C	THR141	electrostatic stabiliser
C	ASP235	electrostatic stabiliser
C	ASP238	modifies pKa

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