Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4YTP

CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH N-[(4-tert-butylphenyl)methyl]-2-(trifluoromethyl)benzamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005759	cellular_component	mitochondrial matrix
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	0007399	biological_process	nervous system development
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	0005515	molecular_function	protein binding
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	0048039	molecular_function	ubiquinone 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	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	0043495	molecular_function	protein-membrane adaptor activity
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	0043495	molecular_function	protein-membrane adaptor activity
D	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
D	0046872	molecular_function	metal ion binding
D	0048039	molecular_function	ubiquinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	binding site for residue FAD A 701

Chain	Residue
A	GLY26
A	SER56
A	HIS57
A	THR58
A	ALA61
A	GLN62
A	GLY63
A	GLY64
A	TYR177
A	PHE178
A	ALA179
A	ALA27
A	THR214
A	GLY215
A	THR225
A	ASP233
A	LEU264
A	HIS365
A	TYR366
A	GLU398
A	ARG409
A	ALA412
A	GLY28
A	ASN413
A	SER414
A	LEU415
A	LEU418
A	GLY29
A	ALA30
A	VAL48
A	THR49
A	LYS50
A	LEU51

site_id	AC2
Number of Residues	6
Details	binding site for residue FES B 301

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

site_id	AC3
Number of Residues	7
Details	binding site for residue SF4 B 302

Chain	Residue
B	CYS158
B	ILE159
B	CYS161
B	ALA162
B	CYS164
B	CYS225
B	PRO226

site_id	AC4
Number of Residues	8
Details	binding site for residue F3S B 303

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

site_id	AC5
Number of Residues	15
Details	binding site for residue HEM C 301

Chain	Residue
C	HIS45
C	ARG46
C	GLY49
C	LEU52
C	SER53
C	VAL56
C	HIS101
C	THR102
C	HIS108
D	ARG47
D	SER50
D	LEU53
D	LEU54
D	HIS79
D	GLY83

site_id	AC6
Number of Residues	9
Details	binding site for residue E23 C 302

Chain	Residue
B	PRO169
B	SER170
B	TRP173
B	HIS216
C	ILE30
C	SER42
C	ARG46
D	ASP90
D	TYR91

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	ARG55-GLY64

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

Chain	Residue	Details
C	ARG24-THR48

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

Chain	Residue	Details
C	HIS101-GLY114

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9YHT1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	19
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Tele-8alpha-FAD histidine","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	10
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	5
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"P31040","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31040","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K2B3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	91
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
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_FI11
Number of Residues	72
Details	Region: {"description":"Interaction with SDHAF1","evidences":[{"source":"UniProtKB","id":"P21912","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZOY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQA3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	136
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	41
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	14
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"15989954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZP0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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