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8SCD

Crystal structure of sulfonamide resistance enzyme Sul3 in complex with reaction intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004156molecular_functiondihydropteroate synthase activity
A0005829cellular_componentcytosol
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016740molecular_functiontransferase activity
A0042558biological_processpteridine-containing compound metabolic process
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. IfGIVNiTtDSFsDgG
ChainResidueDetails
AILE4-GLY19

site_idPS00793
Number of Residues14
DetailsDHPS_2 Dihydropteroate synthase signature 2. GAdVIDLGAasSnP
ChainResidueDetails
AGLY38-PRO51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues255
DetailsDomain: {"description":"Pterin-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00334","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37419898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8SCD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0AC13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"37419898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S2M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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