Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6VAX

Crystal structure of human SDHA-SDHAF2 assembly intermediate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005730	cellular_component	nucleolus
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005749	cellular_component	obsolete mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
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	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
A	0045257	cellular_component	obsolete succinate dehydrogenase complex (ubiquinone)
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	0005730	cellular_component	nucleolus
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0006099	biological_process	tricarboxylic acid cycle
B	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
B	0006470	biological_process	protein dephosphorylation
B	0010719	biological_process	negative regulation of epithelial to mesenchymal transition
B	0018293	biological_process	protein-FAD linkage
B	0034553	biological_process	mitochondrial respiratory chain complex II assembly
B	0090090	biological_process	negative regulation of canonical Wnt signaling pathway
C	0005515	molecular_function	protein binding
C	0005730	cellular_component	nucleolus
C	0005739	cellular_component	mitochondrion
C	0005743	cellular_component	mitochondrial inner membrane
C	0005749	cellular_component	obsolete mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone)
C	0005759	cellular_component	mitochondrial matrix
C	0006099	biological_process	tricarboxylic acid cycle
C	0006105	biological_process	succinate metabolic process
C	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
C	0007399	biological_process	nervous system development
C	0008177	molecular_function	succinate dehydrogenase (quinone) activity
C	0009055	molecular_function	electron transfer activity
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0022900	biological_process	electron transport chain
C	0022904	biological_process	respiratory electron transport chain
C	0042776	biological_process	proton motive force-driven mitochondrial ATP synthesis
C	0045257	cellular_component	obsolete succinate dehydrogenase complex (ubiquinone)
C	0045273	cellular_component	respiratory chain complex II (succinate dehydrogenase)
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0005515	molecular_function	protein binding
D	0005730	cellular_component	nucleolus
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0006099	biological_process	tricarboxylic acid cycle
D	0006121	biological_process	mitochondrial electron transport, succinate to ubiquinone
D	0006470	biological_process	protein dephosphorylation
D	0010719	biological_process	negative regulation of epithelial to mesenchymal transition
D	0018293	biological_process	protein-FAD linkage
D	0034553	biological_process	mitochondrial respiratory chain complex II assembly
D	0090090	biological_process	negative regulation of canonical Wnt signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	binding site for residue FAD A 701

Chain	Residue
A	GLY68
A	HIS99
A	THR100
A	ALA103
A	GLY105
A	GLY106
A	TYR219
A	ALA221
A	ALA255
A	THR256
A	GLY257
A	ALA69
A	SER268
A	ASP275
A	HIS407
A	TYR408
A	GLY439
A	GLU440
A	ALA454
A	SER456
A	LEU457
A	LEU460
A	GLY70
A	OAA702
A	HOH803
A	HOH819
A	GLY71
A	ALA72
A	THR91
A	LYS92
A	LEU93
A	SER98

site_id	AC2
Number of Residues	8
Details	binding site for residue OAA A 702

Chain	Residue
A	PHE173
A	HIS296
A	LEU306
A	ARG340
A	HIS407
A	ARG451
A	ALA454
A	FAD701

site_id	AC3
Number of Residues	5
Details	binding site for residue MLI A 703

Chain	Residue
A	HIS621
A	ARG623
A	PRO643
A	VAL644
A	ASP646

site_id	AC4
Number of Residues	3
Details	binding site for residue GOL A 704

Chain	Residue
A	PHE295
A	ASP341
A	ALA591

site_id	AC5
Number of Residues	6
Details	binding site for residue K A 705

Chain	Residue
A	ASN409
A	MET410
A	GLY411
A	GLU440
A	ALA442
A	HOH801

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO A 706

Chain	Residue
A	ASP131
A	SER588
A	ARG589
A	ARG600
A	ARG662
A	TYR664

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO A 707

Chain	Residue
A	ARG600
A	ILE601
A	ASP602
A	TYR604
A	ASP605
A	LYS616

site_id	AC8
Number of Residues	1
Details	binding site for residue EDO A 708

Chain	Residue
A	GLU583

site_id	AC9
Number of Residues	1
Details	binding site for residue EDO A 709

Chain	Residue
A	THR638

site_id	AD1
Number of Residues	3
Details	binding site for residue GOL C 701

Chain	Residue
C	ARG623
C	PRO643
C	VAL644

site_id	AD2
Number of Residues	6
Details	binding site for residue OAA C 703

Chain	Residue
C	HIS296
C	LEU306
C	ARG340
C	HIS407
C	ARG451
C	FAD702

site_id	AD3
Number of Residues	6
Details	binding site for residue K C 704

Chain	Residue
C	ASN409
C	MET410
C	GLY411
C	GLU440
C	ALA442
C	HOH806

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO C 705

Chain	Residue
C	THR638
C	GLU640

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO C 706

Chain	Residue
C	GLN533
C	CYS536
C	GLU583

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO C 707

Chain	Residue
C	ARG75
C	GLY79
C	GLU82
C	GLU472
C	HOH803

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO C 708

Chain	Residue
C	ASP131
C	SER588
C	LYS598
C	ARG600
C	ARG662
C	TYR664

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO C 709

Chain	Residue
C	ASP341
C	VAL525
C	ALA591

site_id	AD9
Number of Residues	33
Details	binding site for Di-peptide FAD C 702 and HIS C 99

Chain	Residue
C	GLY68
C	ALA69
C	GLY70
C	GLY71
C	ALA72
C	THR91
C	LYS92
C	LEU93
C	SER98
C	THR100
C	VAL101
C	ALA102
C	ALA103
C	GLY105
C	GLY106
C	TYR219
C	ALA221
C	ALA255
C	THR256
C	GLY257
C	THR267
C	SER268
C	ASP275
C	TYR408
C	GLY439
C	GLU440
C	ALA454
C	SER456
C	LEU457
C	LEU460
C	OAA703
C	HOH804
D	GLY78

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG97-GLY106

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250\|UniProtKB:Q9YHT1

Chain	Residue	Details
A	ARG340
C	ARG340

site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q0QF01

Chain	Residue	Details
A	GLY68
C	GLY68
C	THR91
C	ASP275
C	HIS296
C	THR308
C	HIS407
C	GLU440
C	ARG451
C	SER456
A	THR91
A	ASP275
A	HIS296
A	THR308
A	HIS407
A	GLU440
A	ARG451
A	SER456

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Tele-8alpha-FAD histidine => ECO:0000250\|UniProtKB:Q0QF01

Chain	Residue	Details
A	HIS99
C	HIS99

site_id	SWS_FT_FI4
Number of Residues	18
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q8K2B3

Chain	Residue	Details
A	LYS167
C	LYS167
C	LYS182
C	LYS480
C	LYS517
C	LYS550
C	LYS598
C	LYS624
C	LYS636
C	LYS647
A	LYS182
A	LYS480
A	LYS517
A	LYS550
A	LYS598
A	LYS624
A	LYS636
A	LYS647

site_id	SWS_FT_FI5
Number of Residues	14
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q8K2B3

Chain	Residue	Details
A	LYS179
C	LYS335
C	LYS485
C	LYS498
C	LYS538
C	LYS547
A	LYS250
A	LYS335
A	LYS485
A	LYS498
A	LYS538
A	LYS547
C	LYS179
C	LYS250

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269\|PubMed:22823520

Chain	Residue	Details
A	TYR215
C	TYR215

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS541
A	LYS608
C	LYS541
C	LYS608

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q8K2B3

Chain	Residue	Details
A	LYS615
C	LYS615

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