7KYY

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM697 (3-methyl-N-(1-(5-methylisoxazol-3-yl)ethyl)-4-(6-(trifluoromethyl)-1H-indol-3-yl)-1H-pyrrole-2-carboxamide)

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
C	0004152	molecular_function	dihydroorotate dehydrogenase activity
C	0005737	cellular_component	cytoplasm
C	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
C	0016020	cellular_component	membrane
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0004152	molecular_function	dihydroorotate dehydrogenase activity
D	0005737	cellular_component	cytoplasm
D	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
D	0016020	cellular_component	membrane
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue XCD A 1001

Chain	Residue
A	TYR168
A	ILE263
A	ARG265
A	TYR528
A	LEU531
A	VAL532
A	GLY535
A	MET536
A	HOH1235
A	PHE171
A	LEU172
A	GLY181
A	GLU182
A	CYS184
A	HIS185
A	LEU191
A	GLY226

---

site_id	AC2
Number of Residues	21
Details	binding site for residue FMN A 1002

Chain	Residue
A	ALA224
A	ALA225
A	GLY226
A	THR249
A	ASN274
A	ASN342
A	LYS429
A	SER457
A	SER477
A	GLY478
A	LEU481
A	SER505
A	GLY506
A	GLY507
A	TYR528
A	SER529
A	ORO1003
A	HOH1124
A	HOH1151
A	HOH1158
A	HOH1166

---

site_id	AC3
Number of Residues	10
Details	binding site for residue ORO A 1003

Chain	Residue
A	ASN274
A	CYS276
A	GLY277
A	PHE278
A	ASN342
A	SER345
A	ASN347
A	ASN458
A	THR459
A	FMN1002

---

site_id	AC4
Number of Residues	14
Details	binding site for residue XCD B 1001

Chain	Residue
B	TYR168
B	PHE171
B	LEU172
B	GLY181
B	GLU182
B	CYS184
B	HIS185
B	LEU187
B	LEU191
B	ILE263
B	ARG265
B	TYR528
B	LEU531
B	VAL532

---

site_id	AC5
Number of Residues	22
Details	binding site for residue FMN B 1002

Chain	Residue
B	ALA224
B	ALA225
B	GLY226
B	LYS229
B	THR249
B	ASN274
B	ASN342
B	LYS429
B	SER457
B	SER477
B	GLY478
B	LEU481
B	SER505
B	GLY506
B	GLY507
B	TYR528
B	SER529
B	ORO1003
B	HOH1114
B	HOH1115
B	HOH1128
B	HOH1149

---

site_id	AC6
Number of Residues	11
Details	binding site for residue ORO B 1003

Chain	Residue
B	LYS229
B	ASN274
B	CYS276
B	GLY277
B	PHE278
B	ASN342
B	SER345
B	ASN347
B	ASN458
B	THR459
B	FMN1002

---

site_id	AC7
Number of Residues	17
Details	binding site for residue XCD C 1001

Chain	Residue
C	GLY181
C	GLU182
C	CYS184
C	HIS185
C	LEU187
C	PHE188
C	LEU191
C	GLY226
C	ILE263
C	ARG265
C	TYR528
C	LEU531
C	VAL532
C	TYR168
C	PHE171
C	LEU172
C	CYS175

---

site_id	AC8
Number of Residues	23
Details	binding site for residue FMN C 1002

Chain	Residue
C	ALA224
C	ALA225
C	GLY226
C	LYS229
C	THR249
C	ASN274
C	ASN342
C	LYS429
C	SER457
C	ASN458
C	SER477
C	GLY478
C	LEU481
C	SER505
C	GLY506
C	GLY507
C	TYR528
C	SER529
C	ORO1003
C	HOH1107
C	HOH1118
C	HOH1121
C	HOH1136

---

site_id	AC9
Number of Residues	11
Details	binding site for residue ORO C 1003

Chain	Residue
C	LYS229
C	ASN274
C	CYS276
C	GLY277
C	PHE278
C	ASN342
C	SER345
C	ASN347
C	ASN458
C	THR459
C	FMN1002

---

site_id	AD1
Number of Residues	17
Details	binding site for residue XCD D 1001

Chain	Residue
D	TYR168
D	PHE171
D	LEU172
D	GLY181
D	GLU182
D	CYS184
D	HIS185
D	LEU187
D	PHE188
D	LEU191
D	GLY226
D	ILE263
D	ARG265
D	TYR528
D	LEU531
D	VAL532
D	HOH1168

---

site_id	AD2
Number of Residues	20
Details	binding site for residue FMN D 1002

Chain	Residue
D	ALA224
D	ALA225
D	GLY226
D	THR249
D	ASN274
D	ASN342
D	LYS429
D	SER457
D	SER477
D	GLY478
D	SER505
D	GLY506
D	GLY507
D	TYR528
D	SER529
D	ORO1003
D	HOH1107
D	HOH1111
D	HOH1123
D	HOH1139

---

site_id	AD3
Number of Residues	10
Details	binding site for residue ORO D 1003

Chain	Residue
D	ASN274
D	CYS276
D	GLY277
D	PHE278
D	ASN342
D	SER345
D	ASN347
D	ASN458
D	THR459
D	FMN1002

---

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	ILE502-ALA522

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	40
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	32
Details	Binding site: {}

Chain

Residue

Details

---