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5U0Z

E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative

Functional Information from GO Data
ChainGOidnamespacecontents
A0004156molecular_functiondihydropteroate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009396biological_processfolic acid-containing compound biosynthetic process
A0009410biological_processresponse to xenobiotic stimulus
A0016740molecular_functiontransferase activity
A0042558biological_processpteridine-containing compound metabolic process
A0044237biological_processcellular metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046872molecular_functionmetal ion binding
B0004156molecular_functiondihydropteroate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009396biological_processfolic acid-containing compound biosynthetic process
B0009410biological_processresponse to xenobiotic stimulus
B0016740molecular_functiontransferase activity
B0042558biological_processpteridine-containing compound metabolic process
B0044237biological_processcellular metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 7PM A 301
ChainResidue
ATHR62
AHOH463
AASN115
AMET139
AASP185
APHE190
AGLY217
ALYS221
AARG255
AHOH409

site_idAC2
Number of Residues11
Detailsbinding site for residue 7PM B 301
ChainResidue
BASN115
BMET139
BASP185
BPHE190
BGLY217
BLYS221
BARG255
BHOH408
BHOH423
BHOH430
BHOH438

Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. VmGILNvTpDSFsDgG
ChainResidueDetails
AVAL17-GLY32

site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAtIIDVGGesTrP
ChainResidueDetails
AGLY51-PRO64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WND1
ChainResidueDetails
AASN22
BASN22

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:9187658, ECO:0007744|PDB:1AJ2
ChainResidueDetails
ATHR62
BASP185
BLYS221
BARG255
AASP96
AASN115
AASP185
ALYS221
AARG255
BTHR62
BASP96
BASN115

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 394
ChainResidueDetails
ALYS221activator
AARG255activator

site_idMCSA2
Number of Residues2
DetailsM-CSA 394
ChainResidueDetails
BLYS221activator
BARG255activator

226707

PDB entries from 2024-10-30

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