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9BPL

Crystal structure of Adenylosuccinate Lyase from Leishmania major

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006163biological_processpurine nucleotide metabolic process
A0006188biological_processIMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0009152biological_processpurine ribonucleotide biosynthetic process
A0044208biological_process'de novo' AMP biosynthetic process
A0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
B0003824molecular_functioncatalytic activity
B0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006163biological_processpurine nucleotide metabolic process
B0006188biological_processIMP biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0009152biological_processpurine ribonucleotide biosynthetic process
B0044208biological_process'de novo' AMP biosynthetic process
B0070626molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsaMpHKvN
ChainResidueDetails
AGLY320-ASN329

253795

PDB entries from 2026-05-20

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