7KYK

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM589 (ethyl 3-methyl-4-((4-(trifluoromethyl)benzo[d]oxazol-7-yl)methyl)-1H-pyrrole-2-carboxylate)

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	12
Details	binding site for residue XAJ A 1001

Chain	Residue
A	TYR168
A	LEU531
A	VAL532
A	GLY535
A	PHE171
A	GLY181
A	CYS184
A	HIS185
A	LEU187
A	LEU191
A	ILE263
A	ARG265

---

site_id	AC2
Number of Residues	20
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	SER505
A	GLY506
A	GLY507
A	TYR528
A	SER529
A	ORO1003
A	HOH1111
A	HOH1116
A	HOH1140
A	HOH1151

---

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	13
Details	binding site for residue XAJ B 1001

Chain	Residue
B	TYR168
B	PHE171
B	LEU172
B	CYS175
B	GLY181
B	HIS185
B	LEU187
B	LEU191
B	ILE263
B	ARG265
B	LEU531
B	VAL532
B	GLY535

---

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	ASN458
B	SER477
B	GLY478
B	SER505
B	GLY506
B	GLY507
B	TYR528
B	SER529
B	ORO1003
B	HOH1105
B	HOH1113
B	HOH1130
B	HOH1137

---

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	14
Details	binding site for residue XAJ C 1001

Chain	Residue
C	LEU531
C	VAL532
C	GLY535
C	TYR168
C	PHE171
C	LEU172
C	CYS175
C	GLY181
C	CYS184
C	HIS185
C	LEU187
C	LEU191
C	ILE263
C	ARG265

---

site_id	AC8
Number of Residues	21
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	SER477
C	GLY478
C	SER505
C	GLY506
C	GLY507
C	TYR528
C	SER529
C	ORO1003
C	HOH1112
C	HOH1113
C	HOH1120
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	15
Details	binding site for residue XAJ D 1001

Chain	Residue
D	TYR168
D	PHE171
D	LEU172
D	CYS175
D	GLY181
D	CYS184
D	HIS185
D	LEU187
D	PHE188
D	LEU191
D	ILE263
D	ARG265
D	LEU531
D	VAL532
D	GLY535

---

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	ASN458
D	SER477
D	GLY478
D	SER505
D	GLY506
D	GLY507
D	TYR528
D	SER529
D	ORO1003
D	HOH1102
D	HOH1113
D	HOH1125

---

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	ACT_SITE: Nucleophile => ECO:0000250

Chain	Residue	Details
A	SER345
B	SER345
C	SER345
D	SER345

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:16510978, ECO:0000269|PubMed:20702404

Chain	Residue	Details
A	ALA225
B	GLY507
B	GLY535
B	LEU558
C	ALA225
C	THR249
C	THR459
C	GLY507
C	GLY535
C	LEU558
D	ALA225
A	THR249
D	THR249
D	THR459
D	GLY507
D	GLY535
D	LEU558
A	THR459
A	GLY507
A	GLY535
A	LEU558
B	ALA225
B	THR249
B	THR459

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING:

Chain	Residue	Details
A	LYS229
B	PHE488
C	LYS229
C	ASN274
C	ASN342
C	ASN347
C	PHE488
D	LYS229
D	ASN274
D	ASN342
D	ASN347
A	ASN274
D	PHE488
A	ASN342
A	ASN347
A	PHE488
B	LYS229
B	ASN274
B	ASN342
B	ASN347

---