5U12

E. coli dihydropteroate synthase complexed with an 8-mercaptoguanine derivative: 2-azanyl-8-[(2-fluorophenyl)methylsulfanyl]-1,9-dihydropurin-6-one

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004156	molecular_function	dihydropteroate synthase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009396	biological_process	folic acid-containing compound biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016740	molecular_function	transferase activity
A	0042558	biological_process	pteridine-containing compound metabolic process
A	0044237	biological_process	cellular metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046656	biological_process	folic acid biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0004156	molecular_function	dihydropteroate synthase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009396	biological_process	folic acid-containing compound biosynthetic process
B	0009410	biological_process	response to xenobiotic stimulus
B	0016740	molecular_function	transferase activity
B	0042558	biological_process	pteridine-containing compound metabolic process
B	0044237	biological_process	cellular metabolic process
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046656	biological_process	folic acid biosynthetic process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL17-GLY32

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

Chain	Residue	Details
A	GLY51-PRO64

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P9WND1

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305\|PubMed:9187658, ECO:0007744\|PDB:1AJ2

Catalytic Information from CSA