1DUD

DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDE HYDROLASE (D-UTPASE) COMPLEXED WITH THE SUBSTRATE ANALOGUE DEOXYURIDINE 5'-DIPHOSPHATE (D-UDP)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004170	molecular_function	dUTP diphosphatase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006226	biological_process	dUMP biosynthetic process
A	0009117	biological_process	nucleotide metabolic process
A	0016787	molecular_function	hydrolase activity
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046081	biological_process	dUTP catabolic process
A	0046872	molecular_function	metal ion binding
A	0070207	biological_process	protein homotrimerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DUD A 153

Chain	Residue
A	MET68
A	GLN96
A	MET98
A	GLN119
A	HOH235
A	HOH271
A	HOH359
A	HOH390
A	HOH392
A	SER72
A	GLY73
A	ASN84
A	GLY87
A	LEU88
A	ILE89
A	ASP90
A	TYR93

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER72

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15208312

Chain	Residue	Details
A	LEU85
A	ILE99

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ILE89

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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	ASP90
A	ASP92

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 844

Chain	Residue	Details
A	ALA29	activator
A	ARG71	electrostatic stabiliser
A	GLY73	electrostatic stabiliser
A	ILE80	modifies pKa
A	ASP90	proton acceptor, proton donor

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