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2PTS

Crystal structure of wild type Escherichia coli adenylosuccinate lyase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006188biological_processIMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0006974biological_processDNA damage response
A0009152biological_processpurine ribonucleotide 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
A0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSstMpHKvN
ChainResidueDetails
AGLY294-ASN303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17531264
ChainResidueDetails
AHIS171
ASER295

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:17531264, ECO:0007744|PDB:2PTR
ChainResidueDetails
AARG15
AASN90
ATHR122
AGLN247
ASER296
ALYS301
AASN309
AARG335
ASER340

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17531264, ECO:0007744|PDB:2PTQ
ChainResidueDetails
AHIS91

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS94
ALYS366

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AGLU308
ALYS301

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ATHR170
AHIS171

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AHIS171

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AGLU311
ALYS301

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PDB entries from 2024-07-31

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