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1C3C

T. MARITIMA 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
B0003824molecular_functioncatalytic activity
B0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0009152biological_processpurine ribonucleotide biosynthetic process
B0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
B0016829molecular_functionlyase activity
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. GSsaMpHKkN
ChainResidueDetails
AGLY261-ASN270

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10673438
ChainResidueDetails
AHIS141

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
ASER262

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
AARG4
AASN67
ATHR93
AGLN212
ASER263
ALYS268
ASER307

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 80
ChainResidueDetails
AHIS68electrostatic stabiliser
ATHR140electrostatic stabiliser
AHIS141hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER263proton acceptor, proton donor
ALYS268electrostatic stabiliser
AGLU275activator, hydrogen bond acceptor, increase basicity

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PDB entries from 2024-04-24

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