7S87

Crystal Structure of Dihydroorotate dehydrogenase from Plasmodium falciparum in complex with Orotate, FMN, and inhibitor NCGC00600348-01

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004152	molecular_function	dihydroorotate dehydrogenase activity
A	0005737	cellular_component	cytoplasm
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0016020	cellular_component	membrane
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0004152	molecular_function	dihydroorotate dehydrogenase activity
B	0005737	cellular_component	cytoplasm
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0016020	cellular_component	membrane
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors

Functional Information from PROSITE/UniProt

site_id	PS00911
Number of Residues	20
Details	DHODEHASE_1 Dihydroorotate dehydrogenase signature 1. SfieiGTITprgQtGNakPR

Chain	Residue	Details
A	SER243-ARG262

---

site_id	PS00912
Number of Residues	21
Details	DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIAsGGIfSgldAleKIeAGA

Chain	Residue	Details
A	ILE472-ALA492

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16510978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20702404","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---