Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4YSY

Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with N-[(2,4-dichlorophenyl)methyl]-2-(trifluoromethyl)benzamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006099	biological_process	tricarboxylic acid cycle
A	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
A	0008177	molecular_function	succinate dehydrogenase (quinone) activity
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0022900	biological_process	electron transport chain
A	0031966	cellular_component	mitochondrial membrane
A	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006099	biological_process	tricarboxylic acid cycle
B	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
B	0008177	molecular_function	succinate dehydrogenase (quinone) activity
B	0009055	molecular_function	electron transfer activity
B	0009060	biological_process	aerobic respiration
B	0016491	molecular_function	oxidoreductase activity
B	0022904	biological_process	respiratory electron transport chain
B	0031966	cellular_component	mitochondrial membrane
B	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0051538	molecular_function	3 iron, 4 sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0006099	biological_process	tricarboxylic acid cycle
C	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
C	0009055	molecular_function	electron transfer activity
C	0016020	cellular_component	membrane
C	0020037	molecular_function	heme binding
C	0031966	cellular_component	mitochondrial membrane
C	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
C	0046872	molecular_function	metal ion binding
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005740	cellular_component	mitochondrial envelope
D	0005743	cellular_component	mitochondrial inner membrane
D	0006099	biological_process	tricarboxylic acid cycle
D	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
D	0016020	cellular_component	membrane
D	0020037	molecular_function	heme binding
D	0031966	cellular_component	mitochondrial membrane
D	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
D	0046872	molecular_function	metal ion binding
D	0048039	molecular_function	ubiquinone binding
E	0000166	molecular_function	nucleotide binding
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005743	cellular_component	mitochondrial inner membrane
E	0006099	biological_process	tricarboxylic acid cycle
E	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
E	0008177	molecular_function	succinate dehydrogenase (quinone) activity
E	0009055	molecular_function	electron transfer activity
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0022900	biological_process	electron transport chain
E	0031966	cellular_component	mitochondrial membrane
E	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005743	cellular_component	mitochondrial inner membrane
F	0006099	biological_process	tricarboxylic acid cycle
F	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
F	0008177	molecular_function	succinate dehydrogenase (quinone) activity
F	0009055	molecular_function	electron transfer activity
F	0009060	biological_process	aerobic respiration
F	0016491	molecular_function	oxidoreductase activity
F	0022904	biological_process	respiratory electron transport chain
F	0031966	cellular_component	mitochondrial membrane
F	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0051538	molecular_function	3 iron, 4 sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0005515	molecular_function	protein binding
G	0005739	cellular_component	mitochondrion
G	0005743	cellular_component	mitochondrial inner membrane
G	0006099	biological_process	tricarboxylic acid cycle
G	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
G	0009055	molecular_function	electron transfer activity
G	0016020	cellular_component	membrane
G	0020037	molecular_function	heme binding
G	0031966	cellular_component	mitochondrial membrane
G	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
G	0046872	molecular_function	metal ion binding
H	0005515	molecular_function	protein binding
H	0005739	cellular_component	mitochondrion
H	0005740	cellular_component	mitochondrial envelope
H	0005743	cellular_component	mitochondrial inner membrane
H	0006099	biological_process	tricarboxylic acid cycle
H	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
H	0016020	cellular_component	membrane
H	0020037	molecular_function	heme binding
H	0031966	cellular_component	mitochondrial membrane
H	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
H	0046872	molecular_function	metal ion binding
H	0048039	molecular_function	ubiquinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue MLI A 701

Chain	Residue
A	GLY85
A	FAD702
A	PHE153
A	HIS276
A	LEU286
A	THR288
A	GLU289
A	ARG320
A	HIS387
A	ARG432

site_id	AC2
Number of Residues	35
Details	binding site for residue FAD A 702

Chain	Residue
A	GLY48
A	ALA49
A	GLY50
A	GLY51
A	ALA52
A	VAL70
A	THR71
A	LYS72
A	MET73
A	SER78
A	HIS79
A	THR80
A	ALA82
A	ALA83
A	GLN84
A	GLY85
A	GLY86
A	TYR199
A	ALA201
A	ALA235
A	THR236
A	GLY237
A	THR247
A	ASP255
A	LEU286
A	HIS387
A	TYR388
A	GLY420
A	GLU421
A	ARG432
A	ALA435
A	SER437
A	LEU438
A	MLI701
A	HOH801

site_id	AC3
Number of Residues	6
Details	binding site for residue FES B 301

Chain	Residue
B	SER88
B	CYS89
B	CYS94
B	GLY95
B	CYS97
B	CYS109

site_id	AC4
Number of Residues	4
Details	binding site for residue SF4 B 302

Chain	Residue
B	CYS182
B	CYS185
B	CYS188
B	CYS249

site_id	AC5
Number of Residues	8
Details	binding site for residue F3S B 303

Chain	Residue
B	CYS192
B	TYR202
B	CYS239
B	HIS240
B	MET243
B	ASN244
B	CYS245
B	ALA256

site_id	AC6
Number of Residues	10
Details	binding site for residue E24 B 304

Chain	Residue
B	PRO193
B	SER194
B	TRP197
B	HIS240
C	TRP69
C	SER72
C	GLY73
C	ARG76
D	ASP106
D	TYR107

site_id	AC7
Number of Residues	16
Details	binding site for residue HEM C 201

Chain	Residue
B	HIS240
C	HIS75
C	ARG76
C	GLY79
C	CYS80
C	MET82
C	ALA83
C	HIS131
C	THR132
D	ARG63
D	ALA66
D	MET69
D	ILE73
D	HIS95
D	VAL96
D	GLY99

site_id	AC8
Number of Residues	11
Details	binding site for residue EPH D 201

Chain	Residue
D	TRP154
C	THR85
C	VAL170
D	VAL70
D	ILE73
D	ALA76
D	TYR77
D	PHE78
D	HIS80
D	PHE150
D	GLU151

site_id	AC9
Number of Residues	12
Details	binding site for residue MLI E 701

Chain	Residue
E	GLN84
E	GLY85
E	PHE153
E	HIS276
E	LEU286
E	THR288
E	GLU289
E	ARG320
E	HIS387
E	ARG432
E	ALA435
E	FAD702

site_id	AD1
Number of Residues	35
Details	binding site for residue FAD E 702

Chain	Residue
E	GLY48
E	ALA49
E	GLY50
E	GLY51
E	ALA52
E	THR71
E	LYS72
E	MET73
E	SER78
E	HIS79
E	THR80
E	ALA82
E	ALA83
E	GLN84
E	GLY85
E	GLY86
E	TYR199
E	ALA201
E	ALA235
E	THR236
E	GLY237
E	THR247
E	ASP255
E	LEU286
E	HIS387
E	TYR388
E	GLY420
E	GLU421
E	ARG432
E	ALA435
E	ASN436
E	SER437
E	LEU438
E	MLI701
E	HOH805

site_id	AD2
Number of Residues	7
Details	binding site for residue FES F 301

Chain	Residue
F	SER88
F	CYS89
F	GLY92
F	CYS94
F	GLY95
F	CYS97
F	CYS109

site_id	AD3
Number of Residues	5
Details	binding site for residue SF4 F 302

Chain	Residue
F	CYS182
F	CYS185
F	ALA186
F	CYS188
F	CYS249

site_id	AD4
Number of Residues	8
Details	binding site for residue F3S F 303

Chain	Residue
F	CYS192
F	TYR202
F	CYS239
F	HIS240
F	THR241
F	MET243
F	ASN244
F	CYS245

site_id	AD5
Number of Residues	10
Details	binding site for residue E24 F 304

Chain	Residue
F	PRO193
F	SER194
F	TRP197
F	HIS240
G	TRP69
G	SER72
G	GLY73
G	ARG76
H	ASP106
H	TYR107

site_id	AD6
Number of Residues	15
Details	binding site for residue HEM G 201

Chain	Residue
F	HIS240
G	HIS75
G	ARG76
G	GLY79
G	CYS80
G	MET82
G	ALA83
G	HIS131
G	THR132
H	ARG63
H	ALA66
H	ILE73
H	HIS95
H	VAL96
H	GLY99

site_id	AD7
Number of Residues	10
Details	binding site for residue EPH H 201

Chain	Residue
G	THR85
G	VAL170
H	VAL70
H	ILE73
H	ALA76
H	TYR77
H	HIS80
H	PHE150
H	GLU151
H	TRP154

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC

Chain	Residue	Details
B	CYS89-CYS97

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCSaSCP

Chain	Residue	Details
B	CYS182-PRO193

site_id	PS00504
Number of Residues	10
Details	FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTtaAqGG

Chain	Residue	Details
A	ARG77-GLY86

site_id	PS01000
Number of Residues	25
Details	SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPIaphLtiykpqMtwmvSglHRvT

Chain	Residue	Details
C	ARG54-THR78

site_id	PS01001
Number of Residues	14
Details	SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtlnGIRFIgFDmA

Chain	Residue	Details
C	HIS131-ALA144

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PIRSR:PIRSR611281-1

Chain	Residue	Details
A	ARG320
B	CYS245
B	CYS249
F	CYS89
F	CYS94
F	CYS97
F	CYS109
F	CYS182
F	CYS185
F	CYS188
F	CYS192
E	ARG320
F	CYS239
F	CYS245
F	CYS249
H	GLY26-PHE59
H	ASN105-ALA119
B	CYS182
B	CYS185
B	CYS188
B	CYS192
B	CYS239

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0000269\|PubMed:26198225, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VR9, ECO:0007744\|PDB:3VRA, ECO:0007744\|PDB:3VRB, ECO:0007744\|PDB:4YSX, ECO:0007744\|PDB:4YSY, ECO:0007744\|PDB:4YSZ, ECO:0007744\|PDB:4YT0, ECO:0007744\|PDB:4YTM, ECO:0007744\|PDB:4YTN, ECO:0007744\|PDB:5C2T, ECO:0007744\|PDB:5C3J

Chain	Residue	Details
A	ALA49
E	THR71
E	SER78
E	THR80
E	GLY86
E	ALA201
E	SER437
E	LEU438
A	THR71
A	SER78
A	THR80
A	GLY86
A	ALA201
A	SER437
A	LEU438
E	ALA49

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0000269\|PubMed:26198225, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VRA, ECO:0007744\|PDB:4YSX, ECO:0007744\|PDB:4YSY, ECO:0007744\|PDB:4YSZ, ECO:0007744\|PDB:4YT0, ECO:0007744\|PDB:4YTM, ECO:0007744\|PDB:4YTN, ECO:0007744\|PDB:5C2T, ECO:0007744\|PDB:5C3J

Chain	Residue	Details
A	ALA52
E	ALA52
H	ILE79-GLU83
H	HIS142-LEU156

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0000269\|PubMed:26198225, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VR9, ECO:0007744\|PDB:3VRB, ECO:0007744\|PDB:4YSX, ECO:0007744\|PDB:4YSY, ECO:0007744\|PDB:4YT0

Chain	Residue	Details
A	LYS72
E	LYS72
G	SER72
G	ARG76

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0000269\|PubMed:26198225, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VR9, ECO:0007744\|PDB:3VRA, ECO:0007744\|PDB:3VRB, ECO:0007744\|PDB:4YSX, ECO:0007744\|PDB:4YSY, ECO:0007744\|PDB:4YSZ, ECO:0007744\|PDB:4YT0, ECO:0007744\|PDB:4YTN, ECO:0007744\|PDB:5C2T

Chain	Residue	Details
A	GLN84
E	GLN84

site_id	SWS_FT_FI6
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VRB

Chain	Residue	Details
A	GLY85
E	ARG432
A	HIS276
A	THR288
A	GLU289
A	ARG432
E	GLY85
E	HIS276
E	THR288
E	GLU289

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0000269\|PubMed:26198225, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:4YSX, ECO:0007744\|PDB:4YSY, ECO:0007744\|PDB:4YSZ, ECO:0007744\|PDB:4YT0, ECO:0007744\|PDB:4YTM, ECO:0007744\|PDB:5C2T, ECO:0007744\|PDB:5C3J

Chain	Residue	Details
A	ASP255
E	ASP255

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0007744\|PDB:3VRB

Chain	Residue	Details
A	HIS387
A	ALA435
E	HIS387
E	ALA435

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22577165, ECO:0000269\|PubMed:26198225, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VR9, ECO:0007744\|PDB:3VRA, ECO:0007744\|PDB:3VRB, ECO:0007744\|PDB:4YSX, ECO:0007744\|PDB:4YSY, ECO:0007744\|PDB:4YSZ, ECO:0007744\|PDB:4YT0, ECO:0007744\|PDB:4YTN, ECO:0007744\|PDB:5C2T, ECO:0007744\|PDB:5C3J

Chain	Residue	Details
A	GLU421
E	GLU421

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Tele-8alpha-FAD histidine => ECO:0000255\|PIRSR:PIRSR611281-4, ECO:0000269\|PubMed:22577165, ECO:0007744\|PDB:3VR8, ECO:0007744\|PDB:3VR9, ECO:0007744\|PDB:3VRA, ECO:0007744\|PDB:3VRB

Chain	Residue	Details
A	HIS79
E	HIS79

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)