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3BHG

Crystal structure of adenylosuccinate lyase from Legionella pneumophila

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
A0006188biological_processIMP biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG36
AHIS91
AASP92
AVAL93
ASER123
AASN127

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH610
AHIS91
AHIS171
AHOH569

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AASN128
AILE203
APRO204
AGLU249
AHIS251
AILE254
AHOH522
AHOH547
AHOH644

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:0000250|UniProtKB:P0AB89
ChainResidueDetails
AHIS171
ASER295

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0AB89
ChainResidueDetails
ASER296
ALYS301
AASN309
AARG335
ASER340
AARG15
AASN90
ATHR122
AGLN247

221051

PDB entries from 2024-06-12

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