5WRU

Crystal structure of type I inorganic pyrophosphatase from P falciparum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004427	molecular_function	inorganic diphosphate phosphatase activity
A	0005737	cellular_component	cytoplasm
A	0006796	biological_process	phosphate-containing compound metabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004427	molecular_function	inorganic diphosphate phosphatase activity
B	0005737	cellular_component	cytoplasm
B	0006796	biological_process	phosphate-containing compound metabolic process
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004427	molecular_function	inorganic diphosphate phosphatase activity
C	0005737	cellular_component	cytoplasm
C	0006796	biological_process	phosphate-containing compound metabolic process
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004427	molecular_function	inorganic diphosphate phosphatase activity
D	0005737	cellular_component	cytoplasm
D	0006796	biological_process	phosphate-containing compound metabolic process
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0004427	molecular_function	inorganic diphosphate phosphatase activity
E	0005737	cellular_component	cytoplasm
E	0006796	biological_process	phosphate-containing compound metabolic process
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue PO4 C 401

Chain	Residue
C	ARG158
C	TYR275
C	LYS276

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site_id	AC2
Number of Residues	9
Details	binding site for Di-peptide PO4 B 401 and ARG B 158

Chain	Residue
B	TYR159
B	TYR275
B	LYS276
A	ASN54
B	LYS136
B	GLN150
B	ASP151
B	LYS156
B	LEU157

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Functional Information from PROSITE/UniProt

site_id	PS00387
Number of Residues	7
Details	PPASE Inorganic pyrophosphatase signature. DNDPLDI

Chain	Residue	Details
A	ASP198-ILE204

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
D	ASP203
D	ASP235
E	ASP198
E	ASP203
E	ASP235
A	ASP198
A	ASP203
B	ASP198
B	ASP203
B	ASP235
C	ASP198
C	ASP203
C	ASP235
D	ASP198
A	ASP235

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