2J4Q

Crystal structure of a E138A Escherichia coli dCTP deaminase mutant enzyme in complex with dTTP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TYD A 194

Chain	Residue
A	ARG110
A	VAL136
A	TYR171
A	SER111
A	SER112
A	ARG115
A	HIS121
A	ALA124
A	ARG126
A	ASP128
A	ILE135

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TTP B 194

Chain	Residue
B	ASP34
B	ARG110
B	SER111
B	SER112
B	ARG115
B	HIS121
B	ALA124
B	HIS125
B	ARG126
B	ASP128
B	ILE135
B	VAL136
B	MG195

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 195

Chain	Residue
B	GLY109
B	ARG126
B	ALA157
B	TTP194

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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

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site_id	SWS_FT_FI2
Number of Residues	4
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
A	VAL136
B	ARG110
B	VAL136

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17651436, ECO:0000305|PubMed:17996716

Chain	Residue	Details
A	ALA124
B	ALA124

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716

Chain	Residue	Details
A	TYR171
B	TYR171

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:15539408, ECO:0000305|PubMed:17996716

Chain	Residue	Details
A	LYS178
A	GLN182
B	LYS178
B	GLN182

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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

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

Chain	Residue	Details
B	GLY130
B	ASP128

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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

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