Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6MYS

Avian mitochondrial complex II with Atpenin A5 bound, sidechain outside

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005743	cellular_component	mitochondrial inner membrane
A	0006099	biological_process	tricarboxylic acid cycle
A	0006105	biological_process	succinate metabolic process
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	0022904	biological_process	respiratory electron transport chain
A	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0006099	biological_process	tricarboxylic acid cycle
B	0009055	molecular_function	electron transfer activity
B	0016491	molecular_function	oxidoreductase activity
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0006099	biological_process	tricarboxylic acid cycle
C	0009055	molecular_function	electron transfer activity
C	0016020	cellular_component	membrane
C	0046872	molecular_function	metal ion binding
D	0005740	cellular_component	mitochondrial envelope
D	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	37
Details	binding site for residue FAD A 1001

Chain	Residue
A	GLY25
A	SER55
A	HIS56
A	THR57
A	ALA59
A	ALA60
A	GLN61
A	GLY62
A	GLY63
A	TYR176
A	PHE177
A	ALA26
A	ALA178
A	ALA212
A	THR213
A	GLY214
A	ASP232
A	LEU263
A	HIS364
A	TYR365
A	GLY396
A	GLU397
A	GLY27
A	ARG408
A	ALA411
A	ASN412
A	SER413
A	LEU414
A	LEU417
A	OAA1003
A	HOH1108
A	GLY28
A	ALA29
A	VAL47
A	THR48
A	LYS49
A	LEU50

site_id	AC2
Number of Residues	6
Details	binding site for residue K A 1002

Chain	Residue
A	TYR365
A	ASN366
A	MET367
A	GLY368
A	GLU397
A	ALA399

site_id	AC3
Number of Residues	12
Details	binding site for residue OAA A 1003

Chain	Residue
A	GLY62
A	PHE130
A	HIS253
A	LEU263
A	THR265
A	GLU266
A	ARG297
A	HIS364
A	ARG408
A	GLY410
A	ALA411
A	FAD1001

site_id	AC4
Number of Residues	8
Details	binding site for residue FES B 1001

Chain	Residue
B	SER64
B	CYS65
B	ARG66
B	GLY68
B	CYS70
B	GLY71
B	CYS73
B	CYS85

site_id	AC5
Number of Residues	10
Details	binding site for residue SF4 B 1002

Chain	Residue
B	CYS158
B	ILE159
B	LEU160
B	CYS161
B	ALA162
B	CYS163
B	CYS164
B	MET185
B	CYS225
B	PRO226

site_id	AC6
Number of Residues	10
Details	binding site for residue F3S B 1003

Chain	Residue
B	CYS168
B	TYR178
B	CYS215
B	HIS216
B	THR217
B	ILE218
B	MET219
B	ASN220
B	CYS221
B	ILE235

site_id	AC7
Number of Residues	11
Details	binding site for residue AT5 C 202

Chain	Residue
B	PRO169
B	SER170
B	TRP173
B	HIS216
B	ILE218
C	ILE27
C	MET36
C	SER39
C	ILE40
C	ARG43
D	TYR58

site_id	AC8
Number of Residues	14
Details	binding site for residue HEM C 201

Chain	Residue
C	SER50
C	HIS98
C	THR99
C	HIS105
D	ARG14
D	LEU20
D	LEU43
D	HIS46
D	GLY50
B	HIS216
C	HIS42
C	ARG43
C	GLY46
C	LEU49

site_id	AC9
Number of Residues	8
Details	binding site for residue UMQ C 203

Chain	Residue
B	ARG223
C	TRP32
C	SER33
C	LEU34
C	ALA37
C	GLU120
D	TYR88
D	TYR89

site_id	AD1
Number of Residues	7
Details	binding site for residue 3PE D 201

Chain	Residue
C	LEU95
C	MET140
D	ALA27
D	TYR28
D	VAL97
D	ALA98
D	TRP101

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	CYS65-CYS73

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	CYS158-PRO169

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

Chain	Residue	Details
A	ARG54-GLY63

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

Chain	Residue	Details
C	ARG21-THR45

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

Chain	Residue	Details
C	HIS98-GLY111

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15805592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	93
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	30
Details	Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YQ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H88","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	62
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	20
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16371358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16935256","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YQ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YQ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H88","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H89","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 294

Chain	Residue	Details
A	PHE130	steric role
A	GLN251	electrostatic stabiliser, hydrogen bond acceptor, steric role
A	HIS253	electrostatic stabiliser, hydrogen bond donor, steric role
A	LEU263	steric role
A	GLU266	electrostatic stabiliser, hydrogen bond acceptor, steric role
A	ARG297	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS364	electrostatic stabiliser, hydrogen bond donor, steric role
A	ARG408	electrostatic stabiliser, hydrogen bond donor, steric role

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