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7S2I

Crystal structure of sulfonamide resistance enzyme Sul1 in complex with 6-hydroxymethylpterin

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
B0004156molecular_functiondihydropteroate synthase activity
B0005829cellular_componentcytosol
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016740molecular_functiontransferase activity
B0042558biological_processpteridine-containing compound metabolic process
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00792
Number of Residues16
DetailsDHPS_1 Dihydropteroate synthase signature 1. VfGILNlTeDSFfDeS
ChainResidueDetails
AVAL4-SER19

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

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 Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"C0HMD9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0AC13","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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