Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NEN

Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006099	biological_process	tricarboxylic acid cycle
A	0008177	molecular_function	succinate dehydrogenase (quinone) activity
A	0009055	molecular_function	electron transfer activity
A	0009060	biological_process	aerobic respiration
A	0009061	biological_process	anaerobic respiration
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0019646	biological_process	aerobic electron transport chain
A	0022900	biological_process	electron transport chain
A	0045281	cellular_component	succinate dehydrogenase complex
A	0045282	cellular_component	plasma membrane succinate dehydrogenase complex
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0006099	biological_process	tricarboxylic acid cycle
B	0008177	molecular_function	succinate dehydrogenase (quinone) activity
B	0009055	molecular_function	electron transfer activity
B	0009060	biological_process	aerobic respiration
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0019646	biological_process	aerobic electron transport chain
B	0022904	biological_process	respiratory electron transport chain
B	0045281	cellular_component	succinate dehydrogenase complex
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	0005886	cellular_component	plasma membrane
C	0006099	biological_process	tricarboxylic acid cycle
C	0008177	molecular_function	succinate dehydrogenase (quinone) activity
C	0009055	molecular_function	electron transfer activity
C	0009060	biological_process	aerobic respiration
C	0016020	cellular_component	membrane
C	0017004	biological_process	cytochrome complex assembly
C	0019646	biological_process	aerobic electron transport chain
C	0020037	molecular_function	heme binding
C	0045281	cellular_component	succinate dehydrogenase complex
C	0046872	molecular_function	metal ion binding
C	0048039	molecular_function	ubiquinone binding
D	0005886	cellular_component	plasma membrane
D	0006099	biological_process	tricarboxylic acid cycle
D	0009055	molecular_function	electron transfer activity
D	0009060	biological_process	aerobic respiration
D	0016020	cellular_component	membrane
D	0017004	biological_process	cytochrome complex assembly
D	0019646	biological_process	aerobic electron transport chain
D	0020037	molecular_function	heme binding
D	0045281	cellular_component	succinate dehydrogenase complex
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OAA A 589

Chain	Residue
A	GLY51
A	GLY402
A	FAD601
A	PHE126
A	HIS242
A	THR254
A	GLU255
A	ARG286
A	HIS354
A	ARG399
A	GLY401

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 590

Chain	Residue
A	TYR355
A	MET356
A	MET357
A	GLU388
A	ALA390

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA B 311

Chain	Residue
B	ASP187
B	THR190

site_id	AC4
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD A 601

Chain	Residue
A	GLY14
A	ALA15
A	GLY16
A	GLY17
A	ALA18
A	SER37
A	LYS38
A	SER44
A	HIS45
A	THR46
A	SER48
A	ALA49
A	GLN50
A	GLY51
A	GLY52
A	TRP164
A	TYR165
A	ALA166
A	ALA201
A	THR202
A	GLY203
A	THR213
A	ASN214
A	ASP221
A	LEU252
A	HIS354
A	TYR355
A	GLY387
A	GLU388
A	ARG399
A	GLY402
A	ASN403
A	SER404
A	LEU405
A	LEU408
A	OAA589
A	HOH617

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES B 302

Chain	Residue
B	SER54
B	CYS55
B	ARG56
B	GLY58
B	VAL59
B	CYS60
B	GLY61
B	ASP63
B	CYS75

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 303

Chain	Residue
B	CYS149
B	ILE150
B	CYS152
B	ALA153
B	CYS155
B	LEU176
B	CYS216
B	LEU220

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE F3S B 304

Chain	Residue
B	CYS159
B	PRO172
B	CYS206
B	HIS207
B	SER208
B	ILE209
B	MET210
B	ASN211
B	CYS212
B	THR223

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEM C 305

Chain	Residue
D	GLY75
D	MET76
D	GLN78
B	HIS207
C	HIS30
C	ARG31
C	THR37
C	PHE38
C	HIS84
C	VAL85
C	GLY88
C	ILE89
C	HIS91
C	CDN308
C	HOH311
D	ALA23
D	LEU26
D	THR27
D	ILE68
D	HIS71

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DNT C 306

Chain	Residue
B	PRO160
B	TRP163
B	TRP164
B	HIS207
B	ILE209
C	LEU15
C	PHE20
C	ALA24
C	SER27
C	ILE28
C	ARG31
D	TYR83

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE CDN C 308

Chain	Residue
C	SER51
C	ALA61
C	SER62
C	MET65
C	LEU78
C	ALA82
C	VAL115
C	LEU123
C	VAL126
C	LEU127
C	TRP129
C	HEM305
C	EPH309
D	TYR29
D	ILE30
D	PHE37
D	GLY41
D	LEU43
D	TRP48
D	ILE68
D	HOH124

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EPH C 309

Chain	Residue
C	LYS107
C	LYS111
C	PHE114
C	TRP129
C	CDN308

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ARG9-SER33

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

Chain	Residue	Details
C	HIS84-GLY97

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

Chain	Residue	Details
A	ARG43-GLY52

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

Chain	Residue	Details
B	CYS149-PRO160

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	23
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
D	MET1-ASP15
B	CYS216
D	THR81-ARG90
B	CYS75
B	CYS149
B	CYS152
B	CYS155
B	CYS159
B	CYS206
B	CYS212

site_id	SWS_FT_FI2
Number of Residues	65
Details	TRANSMEM: Helical

Chain	Residue	Details
D	PHE16-PHE36
D	VAL59-LEU80
D	LEU91-VAL115
A	GLU388
A	SER404

site_id	SWS_FT_FI3
Number of Residues	21
Details	TOPO_DOM: Periplasmic => ECO:0000305

Chain	Residue	Details
D	PHE37-LYS58
A	THR254
A	HIS354
A	ARG399

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: axial binding residue

Chain	Residue	Details
D	HIS71

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:12560550

Chain	Residue	Details
D	TYR83

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1d4c

Chain	Residue	Details
A	HIS242
A	ARG286
A	HIS354
A	ARG399

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)