7TQ1

Crystal structure of adaptive laboratory evolved sulfonamide-resistant Dihydropteroate Synthase (DHPS) from Escherichia coli in complex with 6-hydroxymethylpterin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004156	molecular_function	dihydropteroate synthase activity
A	0009396	biological_process	folic acid-containing compound biosynthetic process
A	0042558	biological_process	pteridine-containing compound metabolic process
B	0004156	molecular_function	dihydropteroate synthase activity
B	0009396	biological_process	folic acid-containing compound biosynthetic process
B	0042558	biological_process	pteridine-containing compound metabolic process

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

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9187658","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1AJ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"37419898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TQ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 394

Chain	Residue	Details
A	LYS223	activator
A	ARG257	activator

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 394

Chain	Residue	Details
B	LYS223	activator
B	ARG257	activator

---