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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
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
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 site: {"evidences":[{"source":"UniProtKB","id":"P9WND1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0AC13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37419898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TQ1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

238582

PDB entries from 2025-07-09

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