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1F1O

STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006167biological_processAMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0009152biological_processpurine ribonucleotide biosynthetic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0016829molecular_functionlyase activity
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
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsaMpHKrN
ChainResidueDetails
AGLY261-ASN270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
AHIS141
ASER262

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
AARG4
AARG67
ATHR93
AGLN212
ASER263
ALYS268
AASN276
ASER307

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ALYS268
AGLU275

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ATHR140
AHIS141

237735

PDB entries from 2025-06-18

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