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2PTR

Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate

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
B0003824molecular_functioncatalytic activity
B0004018molecular_functionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006188biological_processIMP biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0006974biological_processDNA damage response
B0009152biological_processpurine ribonucleotide 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
B0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE 2SA B 1100
ChainResidue
AARG15
AASN309
BGLU86
BASN90
BHIS91
BASP92
BTHR122
BSER123
BGLU124
BTHR170
BGLN247
ATYR16
BARG335
BLEU337
BSER340
BTHR341
BARG344
BHOH1226
BHOH1229
BHOH1231
BHOH1313
BHOH1315
AGLY294
BHOH1317
ASER295
ASER296
ATHR297
AMET298
ALYS301
AASN303

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE 2SA B 1200
ChainResidue
AASN90
AHIS91
AASP92
ATHR122
ASER123
AGLU124
ATHR170
AGLN247
AARG335
ASER340
ATHR341
AARG344
AHOH469
AHOH479
AHOH514
AHOH706
BARG15
BTYR16
BMET298
BLYS301
BASN303
BASN309
BHOH1306
BHOH1342

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 Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17531264
ChainResidueDetails
AALA171
ASER295
BALA171
BSER295

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:17531264, ECO:0007744|PDB:2PTR
ChainResidueDetails
AARG15
BARG15
BASN90
BTHR122
BGLN247
BSER296
BLYS301
BASN309
BARG335
BSER340
AASN90
ATHR122
AGLN247
ASER296
ALYS301
AASN309
AARG335
ASER340

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17531264, ECO:0007744|PDB:2PTQ
ChainResidueDetails
AHIS91
BHIS91

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS94
ALYS366
BLYS94
BLYS366

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PDB entries from 2024-04-24

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