2HQU

Human dUTPase in complex with alpha,beta-iminodUTP and magnesium ion

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	0046081	biological_process	dUTP catabolic process
B	0000287	molecular_function	magnesium ion binding
B	0004170	molecular_function	dUTP diphosphatase activity
B	0006226	biological_process	dUMP biosynthetic process
B	0046081	biological_process	dUTP catabolic process
C	0000287	molecular_function	magnesium ion binding
C	0004170	molecular_function	dUTP diphosphatase activity
C	0006226	biological_process	dUMP biosynthetic process
C	0046081	biological_process	dUTP catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 997

Chain	Residue
A	DUP777
A	HOH1012
A	HOH1042

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 998

Chain	Residue
B	DUP777
C	HOH1021
C	HOH1022

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 999

Chain	Residue
C	HOH1029
B	HOH1019
B	HOH1030
C	DUP777

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 998

Chain	Residue
A	ASP95
A	HOH1009
C	ASP95
C	HOH1031

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site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 999

Chain	Residue
C	ILE72
C	LEU74
C	ASP102
C	GLU103
C	TYR105
C	ARG106

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site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE DUP A 777

Chain	Residue
A	ARG85
A	SER86
A	GLY87
A	GLN131
A	MG997
A	HOH1005
A	HOH1012
A	HOH1014
A	HOH1042
A	HOH1046
B	ALA98
B	GLY99
B	VAL100
B	ILE101
B	ASP102
B	TYR105
B	GLY110
B	HOH1001
B	HOH1011
C	PHE158

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site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE DUP B 777

Chain	Residue
A	ALA98
A	GLY99
A	VAL100
A	ILE101
A	ASP102
A	TYR105
A	GLY110
A	HOH999
B	ARG153
B	GLY157
B	PHE158
B	GLY159
B	SER160
B	THR161
B	HOH1000
B	HOH1008
B	HOH1029
C	ARG85
C	SER86
C	GLY87
C	GLN131
C	MG998
C	HOH1022

---

site_id	AC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE DUP C 777

Chain	Residue
A	ARG153
A	GLY157
A	PHE158
A	GLY159
A	SER160
A	THR161
B	ARG85
B	SER86
B	GLY87
B	GLN131
B	MG999
B	HOH1019
B	HOH1030
C	ALA98
C	GLY99
C	VAL100
C	ILE101
C	ASP102
C	TYR105
C	GLY110
C	HOH1000
C	HOH1001
C	HOH1002
C	HOH1003
C	HOH1029

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:8805593, ECO:0000305|PubMed:17880943, ECO:0007744|PDB:1Q5H, ECO:0007744|PDB:2HQU, ECO:0007744|PDB:3EHW

Chain	Residue	Details
A	ARG85
A	ARG153
A	PHE158
B	ARG85
B	ARG153
B	PHE158
C	ARG85
C	ARG153
C	PHE158

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:8805593, ECO:0000305|PubMed:17880943, ECO:0007744|PDB:1Q5H, ECO:0007744|PDB:2HQU, ECO:0007744|PDB:3ARA, ECO:0007744|PDB:3ARN, ECO:0007744|PDB:3EHW

Chain	Residue	Details
A	GLY99
A	GLY110
B	GLY99
B	GLY110
C	GLY99
C	GLY110

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site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER11
B	SER11
C	SER11

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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	ASP102
A	ASP104

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

Chain	Residue	Details
B	ASP102
B	ASP104

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

Chain	Residue	Details
C	ASP102
C	ASP104

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