2XCD

Structure of YncF,the genomic dUTPase from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004170	molecular_function	dUTP diphosphatase activity
A	0006226	biological_process	dUMP biosynthetic process
A	0009117	biological_process	nucleotide metabolic process
A	0016787	molecular_function	hydrolase activity
A	0046081	biological_process	dUTP catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004170	molecular_function	dUTP diphosphatase activity
B	0006226	biological_process	dUMP biosynthetic process
B	0009117	biological_process	nucleotide metabolic process
B	0016787	molecular_function	hydrolase activity
B	0046081	biological_process	dUTP catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004170	molecular_function	dUTP diphosphatase activity
C	0006226	biological_process	dUMP biosynthetic process
C	0009117	biological_process	nucleotide metabolic process
C	0016787	molecular_function	hydrolase activity
C	0046081	biological_process	dUTP catabolic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004170	molecular_function	dUTP diphosphatase activity
D	0006226	biological_process	dUMP biosynthetic process
D	0009117	biological_process	nucleotide metabolic process
D	0016787	molecular_function	hydrolase activity
D	0046081	biological_process	dUTP catabolic process
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0004170	molecular_function	dUTP diphosphatase activity
E	0006226	biological_process	dUMP biosynthetic process
E	0009117	biological_process	nucleotide metabolic process
E	0016787	molecular_function	hydrolase activity
E	0046081	biological_process	dUTP catabolic process
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0004170	molecular_function	dUTP diphosphatase activity
F	0006226	biological_process	dUMP biosynthetic process
F	0009117	biological_process	nucleotide metabolic process
F	0016787	molecular_function	hydrolase activity
F	0046081	biological_process	dUTP catabolic process
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA A 1131

Chain	Residue
A	SER65
E	LYS105

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 146

Chain	Residue
A	HOH2042
B	ASP39

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 1131

Chain	Residue
C	LYS19
C	ASP27
C	ARG109

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site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA C 1132

Chain	Residue
C	SER65
D	LYS105

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 1133

Chain	Residue
C	TYR85
C	PHE91
C	TRP92
C	PHE93

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 1131

Chain	Residue
C	ARG109
C	HOH2106
D	THR15
D	GLY107
D	HOH2014

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG E 1131

Chain	Residue
E	ASP39
E	HOH2047

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL E 145

Chain	Residue
A	LYS19
A	ASP27
A	ARG109
A	HOH2028

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA E 1132

Chain	Residue
A	ARG109
E	THR15
E	GLY107

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL F 1131

Chain	Residue
F	LYS19
F	ASP27
F	ARG109

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA F 1132

Chain	Residue
F	SER65
F	HOH2075

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA B 1131

Chain	Residue
B	THR15
B	GLY107
F	ARG109

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20823546, ECO:0000305|PubMed:23897460

Chain	Residue	Details
A	ASP82
B	ASP82
C	ASP82
D	ASP82
E	ASP82
F	ASP82

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000305|PubMed:20823546, ECO:0007744|PDB:2XCE

Chain	Residue	Details
A	SER64
B	TYR85
B	PHE93
C	SER64
C	ASN76
C	TYR85
C	PHE93
D	SER64
D	ASN76
D	TYR85
D	PHE93
E	SER64
E	ASN76
E	TYR85
E	PHE93
F	SER64
F	ASN76
F	TYR85
F	PHE93
A	ASN76
A	TYR85
A	PHE93
B	SER64
B	ASN76

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