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2X75

Staphylococcus aureus adenylosuccinate lyase

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
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 PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OXL A 1432
ChainResidue
AHIS68
ASER94
AGLN259
AAMP1433
AHOH2022

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMP A 1433
ChainResidue
AASP69
ASER94
ATHR95
AHIS141
AGLN212
AASN276
AARG301
AILE303
ASER306
AARG310
AOXL1432
AHOH2070
AARG4
ATYR5
AARG67
AHIS68

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE P6G A 1434
ChainResidue
AARG85
AALA125
ALYS129
AASN130

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1435
ChainResidue
AALA207
AGLN215
AARG218

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
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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