Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XS1

dCTP deaminase from Escherichia coli in complex with dUTP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005829	cellular_component	cytosol
A	0006226	biological_process	dUMP biosynthetic process
A	0006229	biological_process	dUTP biosynthetic process
A	0006235	biological_process	dTTP biosynthetic process
A	0008829	molecular_function	dCTP deaminase activity
A	0009117	biological_process	nucleotide metabolic process
A	0009314	biological_process	response to radiation
A	0015949	biological_process	nucleobase-containing small molecule interconversion
A	0016787	molecular_function	hydrolase activity
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0070207	biological_process	protein homotrimerization
B	0000166	molecular_function	nucleotide binding
B	0005829	cellular_component	cytosol
B	0006226	biological_process	dUMP biosynthetic process
B	0006229	biological_process	dUTP biosynthetic process
B	0006235	biological_process	dTTP biosynthetic process
B	0008829	molecular_function	dCTP deaminase activity
B	0009117	biological_process	nucleotide metabolic process
B	0009314	biological_process	response to radiation
B	0015949	biological_process	nucleobase-containing small molecule interconversion
B	0016787	molecular_function	hydrolase activity
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0070207	biological_process	protein homotrimerization
C	0000166	molecular_function	nucleotide binding
C	0005829	cellular_component	cytosol
C	0006226	biological_process	dUMP biosynthetic process
C	0006229	biological_process	dUTP biosynthetic process
C	0006235	biological_process	dTTP biosynthetic process
C	0008829	molecular_function	dCTP deaminase activity
C	0009117	biological_process	nucleotide metabolic process
C	0009314	biological_process	response to radiation
C	0015949	biological_process	nucleobase-containing small molecule interconversion
C	0016787	molecular_function	hydrolase activity
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0070207	biological_process	protein homotrimerization
D	0000166	molecular_function	nucleotide binding
D	0005829	cellular_component	cytosol
D	0006226	biological_process	dUMP biosynthetic process
D	0006229	biological_process	dUTP biosynthetic process
D	0006235	biological_process	dTTP biosynthetic process
D	0008829	molecular_function	dCTP deaminase activity
D	0009117	biological_process	nucleotide metabolic process
D	0009314	biological_process	response to radiation
D	0015949	biological_process	nucleobase-containing small molecule interconversion
D	0016787	molecular_function	hydrolase activity
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0070207	biological_process	protein homotrimerization
E	0000166	molecular_function	nucleotide binding
E	0005829	cellular_component	cytosol
E	0006226	biological_process	dUMP biosynthetic process
E	0006229	biological_process	dUTP biosynthetic process
E	0006235	biological_process	dTTP biosynthetic process
E	0008829	molecular_function	dCTP deaminase activity
E	0009117	biological_process	nucleotide metabolic process
E	0009314	biological_process	response to radiation
E	0015949	biological_process	nucleobase-containing small molecule interconversion
E	0016787	molecular_function	hydrolase activity
E	0032991	cellular_component	protein-containing complex
E	0042802	molecular_function	identical protein binding
E	0070207	biological_process	protein homotrimerization
F	0000166	molecular_function	nucleotide binding
F	0005829	cellular_component	cytosol
F	0006226	biological_process	dUMP biosynthetic process
F	0006229	biological_process	dUTP biosynthetic process
F	0006235	biological_process	dTTP biosynthetic process
F	0008829	molecular_function	dCTP deaminase activity
F	0009117	biological_process	nucleotide metabolic process
F	0009314	biological_process	response to radiation
F	0015949	biological_process	nucleobase-containing small molecule interconversion
F	0016787	molecular_function	hydrolase activity
F	0032991	cellular_component	protein-containing complex
F	0042802	molecular_function	identical protein binding
F	0070207	biological_process	protein homotrimerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 1195

Chain	Residue
A	DUT1194
A	HOH2200
A	HOH2245
A	HOH2257

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 2195

Chain	Residue
B	DUT2194
B	HOH3244
B	HOH3247
B	HOH3248

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 3195

Chain	Residue
C	DUT3194
C	HOH3236
B	HOH3245

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 4195

Chain	Residue
D	DUT4194
D	HOH5218
D	HOH5240

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 5195

Chain	Residue
D	HOH5239
E	DUT5194
E	HOH6220
E	HOH6250

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 6195

Chain	Residue
E	HOH6201
E	HOH6236
F	DUT6194
F	HOH6196

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE DUT A 1194

Chain	Residue
A	ALA124
A	HIS125
A	ARG126
A	ASP128
A	ILE135
A	VAL136
A	TYR171
A	ALA177
A	LYS178
A	TYR179
A	GLN182
A	HOH2200
A	HOH2241
A	HOH2243
A	HOH2245
A	HOH2247
A	HOH2249
A	HOH2257
C	ARG110
C	SER111
C	SER112
C	ARG115
C	MG1195
C	HOH3196

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE DUT B 2194

Chain	Residue
A	ARG110
A	SER111
A	SER112
A	ARG115
A	MG2195
B	ALA124
B	ARG126
B	ASP128
B	TRP131
B	ILE135
B	VAL136
B	TYR171
B	ARG174
B	ALA177
B	LYS178
B	TYR179
B	GLN182
B	HOH3197
B	HOH3244
B	HOH3246
B	HOH3247
B	HOH3248
B	HOH3250
B	HOH3253

site_id	AC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE DUT C 3194

Chain	Residue
B	ARG110
B	SER111
B	SER112
B	ARG115
B	MG3195
C	LEU107
C	ALA124
C	HIS125
C	ARG126
C	ASP128
C	TRP131
C	ILE135
C	VAL136
C	TYR171
C	ARG174
C	LYS178
C	TYR179
C	GLN182
C	HOH3199
C	HOH3212
C	HOH3235
C	HOH3236
C	HOH3238

site_id	BC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE DUT D 4194

Chain	Residue
D	VAL136
D	TYR171
D	ARG174
D	ALA177
D	LYS178
D	TYR179
D	GLN182
D	HOH5208
D	HOH5218
D	HOH5229
D	HOH5240
D	HOH5243
F	ARG110
F	SER111
F	SER112
F	ARG115
F	MG4195
F	HOH6244
D	ALA124
D	HIS125
D	ARG126
D	ASP128
D	TRP131
D	ILE135

site_id	BC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE DUT E 5194

Chain	Residue
D	ARG110
D	SER111
D	SER112
D	ARG115
D	MG5195
D	HOH5196
D	HOH5239
E	ALA124
E	HIS125
E	ARG126
E	ASP128
E	TRP131
E	ILE135
E	VAL136
E	TYR171
E	ARG174
E	ALA177
E	LYS178
E	TYR179
E	GLN182
E	HOH6220
E	HOH6250
E	HOH6253
E	HOH6254
E	HOH6256

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE DUT F 6194

Chain	Residue
E	ARG110
E	SER111
E	SER112
E	ARG115
E	MG6195
F	ALA124
F	ARG126
F	ASP128
F	ILE135
F	VAL136
F	TYR171
F	ARG174
F	ALA177
F	LYS178
F	TYR179
F	GLN182
F	HOH6196
F	HOH6221
F	HOH6235
F	HOH6243
F	HOH6245

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17651436","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17651436","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00146","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15539408","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17996716","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15539408

Chain	Residue	Details
A	GLU138

site_id	MCSA1
Number of Residues	5
Details	M-CSA 732

Chain	Residue	Details
A	SER111	electrostatic stabiliser
A	ARG115	electrostatic stabiliser
A	ALA124	electrostatic stabiliser
A	ARG126	steric role
A	GLU138	proton acceptor, proton donor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 732

Chain	Residue	Details
B	SER111	electrostatic stabiliser
B	ARG115	electrostatic stabiliser
B	ALA124	electrostatic stabiliser
B	ARG126	steric role
B	GLU138	proton acceptor, proton donor

site_id	MCSA3
Number of Residues	5
Details	M-CSA 732

Chain	Residue	Details
C	SER111	electrostatic stabiliser
C	ARG115	electrostatic stabiliser
C	ALA124	electrostatic stabiliser
C	ARG126	steric role
C	GLU138	proton acceptor, proton donor

site_id	MCSA4
Number of Residues	5
Details	M-CSA 732

Chain	Residue	Details
D	SER111	electrostatic stabiliser
D	ARG115	electrostatic stabiliser
D	ALA124	electrostatic stabiliser
D	ARG126	steric role
D	GLU138	proton acceptor, proton donor

site_id	MCSA5
Number of Residues	5
Details	M-CSA 732

Chain	Residue	Details
E	SER111	electrostatic stabiliser
E	ARG115	electrostatic stabiliser
E	ALA124	electrostatic stabiliser
E	ARG126	steric role
E	GLU138	proton acceptor, proton donor

site_id	MCSA6
Number of Residues	5
Details	M-CSA 732

Chain	Residue	Details
F	SER111	electrostatic stabiliser
F	ARG115	electrostatic stabiliser
F	ALA124	electrostatic stabiliser
F	ARG126	steric role
F	GLU138	proton acceptor, proton donor

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