5EYV

Crystal Structure of Adenylosuccinate lyase from Schistosoma mansoni in APO form.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004018	molecular_function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
A	0005829	cellular_component	cytosol
A	0006106	biological_process	fumarate metabolic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0006167	biological_process	AMP biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0009152	biological_process	purine ribonucleotide biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0009168	biological_process	purine ribonucleoside monophosphate biosynthetic process
A	0016829	molecular_function	lyase activity
A	0032261	biological_process	purine nucleotide salvage
A	0042802	molecular_function	identical protein binding
A	0044208	biological_process	'de novo' AMP biosynthetic process
A	0044209	biological_process	AMP salvage
A	0051262	biological_process	protein tetramerization
A	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004018	molecular_function	N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B	0005829	cellular_component	cytosol
B	0006106	biological_process	fumarate metabolic process
B	0006166	biological_process	purine ribonucleoside salvage
B	0006167	biological_process	AMP biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0009152	biological_process	purine ribonucleotide biosynthetic process
B	0009165	biological_process	nucleotide biosynthetic process
B	0009168	biological_process	purine ribonucleoside monophosphate biosynthetic process
B	0016829	molecular_function	lyase activity
B	0032261	biological_process	purine nucleotide salvage
B	0042802	molecular_function	identical protein binding
B	0044208	biological_process	'de novo' AMP biosynthetic process
B	0044209	biological_process	AMP salvage
B	0051262	biological_process	protein tetramerization
B	0070626	molecular_function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity

Functional Information from PROSITE/UniProt

site_id	PS00163
Number of Residues	10
Details	FUMARATE_LYASES Fumarate lyases signature. GSsaMpYKrN

Chain	Residue	Details
A	GLY283-ASN292

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28347672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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