Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XS6

dCTP deaminase from Escherichia coli. E138A mutant enzyme 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	3
Details	BINDING SITE FOR RESIDUE MG C 1195

Chain	Residue
A	DUT1194
A	HOH2221
A	HOH2248

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG A 2195

Chain	Residue
B	DUT2194

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

Chain	Residue
C	DUT3194
C	HOH3217
C	HOH3243

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG F 4195

Chain	Residue
D	DUT4194
D	HOH5243

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 5195

Chain	Residue
E	DUT5194
E	HOH6229
E	HOH6236

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

Chain	Residue
E	HOH6232
E	HOH6244
F	DUT6194
F	HOH6222

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 5196

Chain	Residue
D	HOH5267
D	HOH5268
D	HOH5272
E	HOH6264
E	HOH6265
E	HOH6266

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE DUT A 1194

Chain	Residue
A	ALA124
A	ARG126
A	ASP128
A	TRP131
A	ILE135
A	VAL136
A	TYR171
A	ARG174
A	ALA177
A	LYS178
A	TYR179
A	GLN182
A	HOH2197
A	HOH2201
A	HOH2221
A	HOH2248
C	ARG110
C	SER111
C	SER112
C	ARG115
C	MG1195
C	HOH3215

site_id	AC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE DUT B 2194

Chain	Residue
A	ARG110
A	SER111
A	SER112
A	ARG115
A	MG2195
A	HOH2232
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	HOH3200
B	HOH3204

site_id	BC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE DUT C 3194

Chain	Residue
B	ARG110
B	SER111
B	SER112
B	ARG115
B	MG3195
B	HOH3213
C	ALA124
C	ARG126
C	ASP128
C	TRP131
C	ILE135
C	VAL136
C	TYR171
C	ARG174
C	ALA177
C	LYS178
C	TYR179
C	GLN182
C	HOH3199
C	HOH3203
C	HOH3217
C	HOH3243

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE DUT D 4194

Chain	Residue
D	HOH5212
D	HOH5213
D	HOH5243
F	ARG110
F	SER111
F	SER112
F	ARG115
F	MG4195
F	HOH6203
D	ALA124
D	ARG126
D	ASP128
D	TRP131
D	ILE135
D	VAL136
D	TYR171
D	ARG174
D	ALA177
D	LYS178
D	TYR179
D	GLN182
D	HOH5198

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE DUT E 5194

Chain	Residue
D	ARG110
D	SER111
D	SER112
D	ARG115
D	MG5195
D	HOH5203
E	ALA124
E	ARG126
E	ASP128
E	TRP131
E	ILE135
E	VAL136
E	TYR171
E	ARG174
E	ALA177
E	LYS178
E	TYR179
E	GLN182
E	HOH6201
E	HOH6236
E	HOH6237

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE DUT F 6194

Chain	Residue
E	ARG110
E	SER111
E	SER112
E	ARG115
E	MG6195
E	HOH6232
E	HOH6244
F	ALA124
F	ARG126
F	ASP128
F	TRP131
F	ILE135
F	VAL136
F	TYR171
F	ARG174
F	ALA177
F	LYS178
F	TYR179
F	GLN182
F	HOH6201
F	HOH6207
F	HOH6214
F	HOH6222
F	HOH6251

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_00146, ECO:0000305\|PubMed:15539408, ECO:0000305\|PubMed:17996716

Chain	Residue	Details
A	ALA138
B	ALA138
C	ALA138
D	ALA138
E	ALA138
F	ALA138

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00146, ECO:0000305\|PubMed:15539408, ECO:0000305\|PubMed:17651436, ECO:0000305\|PubMed:17996716

Chain	Residue	Details
A	ARG110
E	VAL136
F	ARG110
F	VAL136
A	VAL136
B	ARG110
B	VAL136
C	ARG110
C	VAL136
D	ARG110
D	VAL136
E	ARG110

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305\|PubMed:15539408, ECO:0000305\|PubMed:17651436, ECO:0000305\|PubMed:17996716

Chain	Residue	Details
A	ALA124
B	ALA124
C	ALA124
D	ALA124
E	ALA124
F	ALA124

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305\|PubMed:15539408, ECO:0000305\|PubMed:17996716

Chain	Residue	Details
A	TYR171
B	TYR171
C	TYR171
D	TYR171
E	TYR171
F	TYR171

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00146, ECO:0000305\|PubMed:15539408, ECO:0000305\|PubMed:17996716

Chain	Residue	Details
A	LYS178
E	GLN182
F	LYS178
F	GLN182
A	GLN182
B	LYS178
B	GLN182
C	LYS178
C	GLN182
D	LYS178
D	GLN182
E	LYS178

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1dup

Chain	Residue	Details
A	GLY130
A	ASP128

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1dup

Chain	Residue	Details
B	GLY130
B	ASP128

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1dup

Chain	Residue	Details
C	GLY130
C	ASP128

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1dup

Chain	Residue	Details
D	GLY130
D	ASP128

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1dup

Chain	Residue	Details
E	GLY130
E	ASP128

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1dup

Chain	Residue	Details
F	GLY130
F	ASP128

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	ALA138	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	ALA138	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	ALA138	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	ALA138	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	ALA138	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	ALA138	proton acceptor, proton donor

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