7S2K

Crystal structure of sulfonamide resistance enzyme Sul2 in complex with 7,8-dihydropteroate, magnesium, and pyrophosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004156	molecular_function	dihydropteroate synthase activity
A	0005829	cellular_component	cytosol
A	0009396	biological_process	folic acid-containing compound biosynthetic process
A	0016740	molecular_function	transferase activity
A	0042558	biological_process	pteridine-containing compound metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046656	biological_process	folic acid biosynthetic process
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
B	0004156	molecular_function	dihydropteroate synthase activity
B	0005829	cellular_component	cytosol
B	0009396	biological_process	folic acid-containing compound biosynthetic process
B	0016740	molecular_function	transferase activity
B	0042558	biological_process	pteridine-containing compound metabolic process
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046656	biological_process	folic acid biosynthetic process
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00792
Number of Residues	16
Details	DHPS_1 Dihydropteroate synthase signature 1. IfGIVNiTsDSFsDgG

Chain	Residue	Details
A	ILE7-GLY22

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site_id	PS00793
Number of Residues	14
Details	DHPS_2 Dihydropteroate synthase signature 2. GAdVIDLGPasSnP

Chain	Residue	Details
A	GLY41-PRO54

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	23
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37419898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S2K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AC13","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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