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1C3U

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 PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 432
ChainResidue
ASER306
ASER307
AARG310
AHOH1025
AHOH1148
BARG4
BARG276

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 433
ChainResidue
AHOH1126
ATHR93
ASER94

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 432
ChainResidue
AARG4
AARG276
BSER306
BSER307
BARG310
BHOH2025
BHOH2148

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 433
ChainResidue
BTHR93
BSER94
BHOH2126

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10673438
ChainResidueDetails
AHIS141
BHIS141

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
ASER262
BSER262

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
AARG4
BTHR93
BGLN212
BSER263
BLYS268
BSER307
AASN67
ATHR93
AGLN212
ASER263
ALYS268
ASER307
BARG4
BASN67

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ATHR140
AHIS141
BLYS268
BGLU275

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ALYS268
AGLU275
BTHR140
BHIS141

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 80
ChainResidueDetails
BHIS68electrostatic stabiliser
BTHR140electrostatic stabiliser
BHIS141hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BSER263proton acceptor, proton donor
BLYS268electrostatic stabiliser
BGLU275activator, hydrogen bond acceptor, increase basicity

219140

PDB entries from 2024-05-01

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