Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5LNX

Crystal structure of MmgC, an acyl-CoA dehydrogenase from bacillus subtilis.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0005737	cellular_component	cytoplasm
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
A	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0005737	cellular_component	cytoplasm
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0030435	biological_process	sporulation resulting in formation of a cellular spore
B	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
B	0050660	molecular_function	flavin adenine dinucleotide 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	0030435	biological_process	sporulation resulting in formation of a cellular spore
C	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
C	0050660	molecular_function	flavin adenine dinucleotide 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	0030435	biological_process	sporulation resulting in formation of a cellular spore
D	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0003995	molecular_function	acyl-CoA dehydrogenase activity
E	0005737	cellular_component	cytoplasm
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0030435	biological_process	sporulation resulting in formation of a cellular spore
E	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0003995	molecular_function	acyl-CoA dehydrogenase activity
F	0005737	cellular_component	cytoplasm
F	0016491	molecular_function	oxidoreductase activity
F	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
F	0030435	biological_process	sporulation resulting in formation of a cellular spore
F	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
F	0050660	molecular_function	flavin adenine dinucleotide binding
G	0003995	molecular_function	acyl-CoA dehydrogenase activity
G	0005737	cellular_component	cytoplasm
G	0016491	molecular_function	oxidoreductase activity
G	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
G	0030435	biological_process	sporulation resulting in formation of a cellular spore
G	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
G	0050660	molecular_function	flavin adenine dinucleotide binding
H	0003995	molecular_function	acyl-CoA dehydrogenase activity
H	0005737	cellular_component	cytoplasm
H	0016491	molecular_function	oxidoreductase activity
H	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
H	0030435	biological_process	sporulation resulting in formation of a cellular spore
H	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
H	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL A 401

Chain	Residue
A	SER130
A	MET234
A	ARG241
A	GLU360
A	GLY361
A	FAD404
A	HOH509

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL A 402

Chain	Residue
A	HOH503
B	GLU55
A	LYS42
A	HIS46

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 403

Chain	Residue
A	PHE99
A	GLY224
A	ASP228
A	HIS231
A	ILE232

site_id	AC4
Number of Residues	21
Details	binding site for residue FAD A 404

Chain	Residue
A	PHE121
A	LEU123
A	THR124
A	GLY129
A	SER130
A	PHE154
A	THR156
A	THR207
A	THR362
A	GLU364
A	GOL401
B	ARG266
B	GLN268
B	PHE269
B	ILE273
B	GLN333
B	ILE334
B	GLY336
B	GLY337
B	HOH701
D	GLN277

site_id	AC5
Number of Residues	25
Details	binding site for residue FAD B 401

Chain	Residue
A	ARG266
A	GLN268
A	PHE269
A	ARG271
A	ILE273
A	ASN276
A	ILE279
A	GLN333
A	ILE334
A	GLY336
A	GLY337
A	TYR338
B	PHE121
B	LEU123
B	THR124
B	GLY129
B	SER130
B	PHE154
B	THR156
B	VAL355
B	TYR359
B	THR362
B	GLU364
B	HOH714
C	GLN277

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL C 401

Chain	Residue
B	HIS299
C	HIS295
C	TYR298
C	HIS299

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL C 402

Chain	Residue
C	LEU97
C	TYR98
C	LYS105

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL C 403

Chain	Residue
B	PHE320
C	ARG289
C	PHE320
C	LYS327

site_id	AC9
Number of Residues	22
Details	binding site for residue FAD C 404

Chain	Residue
B	GLN277
C	PHE121
C	LEU123
C	THR124
C	GLY129
C	SER130
C	PHE154
C	THR156
C	THR207
C	THR362
C	GLU364
D	ARG266
D	GLN268
D	PHE269
D	ILE273
D	ASN276
D	ILE279
D	GLN333
D	ILE334
D	GLY336
D	GLY337
D	TYR338

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL D 401

Chain	Residue
A	ARG289
D	GLN319
D	PHE320
D	ASP323

site_id	AD2
Number of Residues	22
Details	binding site for residue FAD D 402

Chain	Residue
A	GLN277
C	ARG266
C	GLN268
C	PHE269
C	ARG271
C	ILE273
C	ASN276
C	GLN333
C	ILE334
C	GLY337
C	TYR338
D	PHE121
D	LEU123
D	THR124
D	GLY129
D	SER130
D	PHE154
D	THR156
D	VAL355
D	TYR359
D	THR362
D	GLU364

site_id	AD3
Number of Residues	23
Details	binding site for residue FAD E 401

Chain	Residue
E	ALA120
E	LEU123
E	THR124
E	GLY129
E	SER130
E	PHE154
E	THR156
E	TYR359
E	THR362
E	GLU364
F	ARG266
F	GLN268
F	PHE269
F	ARG271
F	ILE273
F	ASN276
F	ILE279
F	GLN333
F	ILE334
F	GLY336
F	GLY337
F	TYR338
H	GLN277

site_id	AD4
Number of Residues	1
Details	binding site for residue GOL F 401

Chain	Residue
F	PHE269

site_id	AD5
Number of Residues	21
Details	binding site for residue FAD F 402

Chain	Residue
E	ARG266
E	GLN268
E	PHE269
E	ILE273
E	ASN276
E	ILE279
E	GLN333
E	ILE334
E	GLY337
E	TYR338
F	PHE121
F	LEU123
F	THR124
F	GLY129
F	SER130
F	PHE154
F	THR156
F	THR362
F	GLU364
F	HOH501
G	GLN277

site_id	AD6
Number of Residues	2
Details	binding site for residue GOL G 402

Chain	Residue
G	GLU55
G	GLN56

site_id	AD7
Number of Residues	23
Details	binding site for residue FAD G 403

Chain	Residue
F	GLN277
G	PHE121
G	LEU123
G	THR124
G	GLY129
G	SER130
G	PHE154
G	THR156
G	VAL355
G	TYR359
G	THR362
G	GLU364
G	LEU368
H	ARG266
H	GLN268
H	PHE269
H	ILE273
H	ASN276
H	ILE279
H	GLN333
H	ILE334
H	GLY337
H	TYR338

site_id	AD8
Number of Residues	1
Details	binding site for residue GOL H 401

Chain	Residue
H	HIS231

site_id	AD9
Number of Residues	24
Details	binding site for residue FAD H 402

Chain	Residue
E	GLN277
G	ARG266
G	GLN268
G	PHE269
G	ILE273
G	ASN276
G	ILE279
G	GLN333
G	ILE334
G	GLY336
G	GLY337
G	TYR338
H	PHE121
H	LEU123
H	THR124
H	GLY129
H	SER130
H	PHE154
H	THR156
H	TYR359
H	GLU360
H	THR362
H	GLU364
H	LEU368

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA122-SER134

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

Chain	Residue	Details
A	GLN333-ASP352

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