2FBW

Avian respiratory complex II with carboxin bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005739	cellular_component	mitochondrion
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	0005739	cellular_component	mitochondrion
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
N	0005739	cellular_component	mitochondrion
N	0005743	cellular_component	mitochondrial inner membrane
N	0006099	biological_process	tricarboxylic acid cycle
N	0006105	biological_process	succinate metabolic process
N	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
N	0008177	molecular_function	succinate dehydrogenase (quinone) activity
N	0009055	molecular_function	electron transfer activity
N	0016491	molecular_function	oxidoreductase activity
N	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
N	0022900	biological_process	electron transport chain
N	0022904	biological_process	respiratory electron transport chain
N	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
N	0050660	molecular_function	flavin adenine dinucleotide binding
O	0006099	biological_process	tricarboxylic acid cycle
O	0009055	molecular_function	electron transfer activity
O	0016491	molecular_function	oxidoreductase activity
O	0051536	molecular_function	iron-sulfur cluster binding
O	0051537	molecular_function	2 iron, 2 sulfur cluster binding
P	0005739	cellular_component	mitochondrion
P	0006099	biological_process	tricarboxylic acid cycle
P	0009055	molecular_function	electron transfer activity
P	0016020	cellular_component	membrane
P	0046872	molecular_function	metal ion binding
Q	0005740	cellular_component	mitochondrial envelope
Q	0016020	cellular_component	membrane

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

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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

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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

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:16371358

Chain	Residue	Details
A	ARG297
B	CYS221
B	CYS225
O	CYS65
O	CYS70
O	CYS73
O	CYS85
O	CYS158
O	CYS161
O	CYS164
O	CYS168
N	ARG297
O	CYS215
O	CYS221
O	CYS225
D	ILE65-PHE86
Q	LEU8-LEU29
Q	VAL35-ILE55
Q	ILE65-PHE86
B	CYS164
B	CYS168
B	CYS215

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site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256

Chain	Residue	Details
A	ALA26
A	GLU397
A	SER413
A	LEU414
N	ALA26
N	ALA29
N	THR48
N	LYS49
N	SER55
N	THR57
N	GLY62
A	ALA29
N	ALA178
N	ASP232
N	GLU397
N	SER413
N	LEU414
A	THR48
A	LYS49
A	SER55
A	THR57
A	GLY62
A	ALA178
A	ASP232

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site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256

Chain	Residue	Details
A	HIS253
N	ALA411
A	THR265
A	HIS364
A	ARG408
A	ALA411
N	HIS253
N	THR265
N	HIS364
N	ARG408

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256

Chain	Residue	Details
A	HIS56
N	HIS56

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site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256

Chain	Residue	Details
D	TYR58
Q	TYR58

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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

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site_id	MCSA2
Number of Residues	8
Details	M-CSA 294

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

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