Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FAH

Molecular basis of the flavin-based electron-bifurcating caffeyl-CoA reductase reaction

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0071949	molecular_function	FAD binding
B	0005737	cellular_component	cytoplasm
B	0009055	molecular_function	electron transfer activity
B	0016491	molecular_function	oxidoreductase activity
B	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
B	0071949	molecular_function	FAD binding
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0005737	cellular_component	cytoplasm
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0071949	molecular_function	FAD binding
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0005737	cellular_component	cytoplasm
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0071949	molecular_function	FAD binding
E	0005737	cellular_component	cytoplasm
E	0009055	molecular_function	electron transfer activity
E	0016491	molecular_function	oxidoreductase activity
E	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
E	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0071949	molecular_function	FAD binding
F	0005737	cellular_component	cytoplasm
F	0009055	molecular_function	electron transfer activity
F	0016491	molecular_function	oxidoreductase activity
F	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
F	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue FAD A 401

Chain	Residue
A	GLY283
A	THR327
A	GLY328
A	GLY340
A	ILE341
A	SER342
A	ALA344
A	GLN346
A	HIS347
A	ASN361
A	LYS362
A	MET284
A	GLY378
A	ASP379
A	LEU380
C	TYR346
D	PRO127
D	ARG152
D	GLU198
A	GLY285
A	SER309
A	ARG310
A	ALA311
A	VAL324
A	GLY325
A	GLN326

site_id	AC2
Number of Residues	6
Details	binding site for residue SF4 A 402

Chain	Residue
A	CYS10
A	GLY12
A	CYS13
A	CYS16
A	CYS48
A	ALA52

site_id	AC3
Number of Residues	8
Details	binding site for residue SF4 A 403

Chain	Residue
A	CYS20
A	PRO21
A	ALA37
A	CYS38
A	THR39
A	ASN40
A	CYS41
A	CYS44

site_id	AC4
Number of Residues	25
Details	binding site for residue FAD B 301

Chain	Residue
A	LEU183
A	THR184
A	ARG203
A	ILE214
B	CYS6
B	ALA7
B	LYS8
B	ASP38
B	THR61
B	MET62
B	ALA93
B	ASP94
B	THR95
B	THR98
B	LEU102
B	GLY118
B	GLN120
B	ALA121
B	GLY124
B	ASP125
B	THR126
B	ALA127
B	GLN128
B	VAL129
B	THR223

site_id	AC5
Number of Residues	21
Details	binding site for residue FAD C 401

Chain	Residue
C	PHE122
C	LEU124
C	THR125
C	GLY130
C	SER131
C	PHE155
C	THR157
C	GLN278
C	GLU362
C	GLY363
C	THR364
C	GLN366
D	ARG267
D	GLN269
D	PHE270
D	ILE274
D	PHE277
D	GLN335
D	ILE336
D	GLY338
D	GLY339

site_id	AC6
Number of Residues	2
Details	binding site for residue SO4 C 402

Chain	Residue
C	LYS344
D	LYS344

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 C 403

Chain	Residue
C	GLU324
C	ARG356
D	GLN335

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 C 404

Chain	Residue
C	ASP286
C	LYS290
C	TYR321

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 C 405

Chain	Residue
A	GLN326
C	GLU259
C	TYR346
C	LYS347

site_id	AD1
Number of Residues	4
Details	binding site for residue SO4 C 406

Chain	Residue
C	GLN248
C	TYR361
C	GLU362
C	SER87

site_id	AD2
Number of Residues	20
Details	binding site for residue FAD D 401

Chain	Residue
C	ARG267
C	GLN269
C	PHE270
C	ILE274
C	PHE277
C	ILE280
C	GLN335
C	ILE336
C	GLY339
D	PHE122
D	LEU124
D	THR125
D	GLY130
D	PHE155
D	THR157
D	GLN278
D	TYR361
D	GLU362
D	THR364
D	GLN366

site_id	AD3
Number of Residues	3
Details	binding site for residue SO4 D 402

Chain	Residue
D	VAL84
D	TYR361
D	GLU362

site_id	AD4
Number of Residues	3
Details	binding site for residue SO4 D 403

Chain	Residue
D	GLU19
D	LEU22
D	THR24

site_id	AD5
Number of Residues	24
Details	binding site for residue FAD E 401

Chain	Residue
C	ARG152
C	GLU198
D	TYR346
E	MET284
E	GLY285
E	SER309
E	ARG310
E	ALA311
E	GLN323
E	VAL324
E	GLY325
E	GLN326
E	THR327
E	GLY328
E	GLY340
E	ILE341
E	SER342
E	GLY343
E	GLN346
E	HIS347
E	ASN361
E	LYS362
E	ASP379
E	LEU380

site_id	AD6
Number of Residues	5
Details	binding site for residue SF4 E 402

Chain	Residue
E	CYS10
E	CYS13
E	CYS16
E	CYS48
E	ALA52

site_id	AD7
Number of Residues	7
Details	binding site for residue SF4 E 403

Chain	Residue
E	CYS20
E	PRO21
E	CYS38
E	THR39
E	ASN40
E	CYS41
E	CYS44

site_id	AD8
Number of Residues	24
Details	binding site for residue FAD F 301

Chain	Residue
E	LEU183
E	ARG203
E	ILE214
F	CYS6
F	ALA7
F	LYS8
F	ASP38
F	THR61
F	MET62
F	ALA93
F	ASP94
F	THR95
F	THR98
F	ALA117
F	GLY118
F	GLN120
F	ALA121
F	GLY124
F	ASP125
F	THR126
F	ALA127
F	GLN128
F	VAL129
F	THR223

Functional Information from PROSITE/UniProt

site_id	PS00072
Number of Residues	13
Details	ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. ALTEpgAGSDagG

Chain	Residue	Details
C	ALA123-GLY135

site_id	PS00073
Number of Residues	20
Details	ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiHGGyGYikEykveRmyrD

Chain	Residue	Details
C	GLN335-ASP354

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

Chain	Residue	Details
A	CYS10-PRO21
A	CYS38-PRO49

site_id	PS01065
Number of Residues	21
Details	ETF_BETA Electron transfer flavoprotein beta-subunit signature. VhRqmEDGy.EvIevqlPcLLT

Chain	Residue	Details
B	VAL157-THR177

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P13804","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P15651","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P15651","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P15651","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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