2QLP

Bifunctional dCTP deaminase:dUTPase from Mycobacterium tuberculosis, apo form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006229	biological_process	dUTP biosynthetic process
A	0008829	molecular_function	dCTP deaminase activity
B	0006229	biological_process	dUTP biosynthetic process
B	0008829	molecular_function	dCTP deaminase activity
C	0006229	biological_process	dUTP biosynthetic process
C	0008829	molecular_function	dCTP deaminase activity
D	0006229	biological_process	dUTP biosynthetic process
D	0008829	molecular_function	dCTP deaminase activity
E	0006229	biological_process	dUTP biosynthetic process
E	0008829	molecular_function	dCTP deaminase activity
F	0006229	biological_process	dUTP biosynthetic process
F	0008829	molecular_function	dCTP deaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1PE A 162

Chain	Residue
A	ARG106
A	LEU107
C	ARG41
C	LEU81
C	SER83

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE 1PE A 163

Chain	Residue
A	ARG41

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 1PE B 162

Chain	Residue
C	ARG106
B	ARG41
B	SER83
B	THR127

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 1PE C 162

Chain	Residue
C	GLN65
C	VAL67
C	ASP68

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 1PE D 162

Chain	Residue
D	ARG41
D	GLY82
D	SER83
E	ARG106

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site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 1PE E 162

Chain	Residue
E	ARG41
E	LEU81
E	GLY82
E	THR127

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site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 1PE F 162

Chain	Residue
D	ARG106
F	ARG41
F	SER83

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P28248, ECO:0000255|HAMAP-Rule:MF_00146

Chain	Residue	Details
A	GLU129
B	GLU129
C	GLU129
D	GLU129
E	GLU129
F	GLU129

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|Ref.4

Chain	Residue	Details
A	LYS101
E	GLN148
F	LYS101
F	GLN148
A	GLN148
B	LYS101
B	GLN148
C	LYS101
C	GLN148
D	LYS101
D	GLN148
E	LYS101

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:18164314, ECO:0000305|Ref.4

Chain	Residue	Details
A	ASP119
E	THR127
F	ASP119
F	THR127
A	THR127
B	ASP119
B	THR127
C	ASP119
C	THR127
D	ASP119
D	THR127
E	ASP119

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Important for bifunctional activity => ECO:0000255|HAMAP-Rule:MF_00146, ECO:0000305|PubMed:18164314

Chain	Residue	Details
A	GLY116
B	GLY116
C	GLY116
D	GLY116
E	GLY116
F	GLY116

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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	GLY121
A	ASP119

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

Chain	Residue	Details
B	GLY121
B	ASP119

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

Chain	Residue	Details
C	GLY121
C	ASP119

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

Chain	Residue	Details
D	GLY121
D	ASP119

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

Chain	Residue	Details
E	GLY121
E	ASP119

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

Chain	Residue	Details
F	GLY121
F	ASP119

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