3MPI

Structure of the glutaryl-coenzyme A dehydrogenase glutaryl-CoA complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000166	molecular_function	nucleotide binding
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000166	molecular_function	nucleotide binding
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000166	molecular_function	nucleotide binding
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD A 400

Chain	Residue
A	PHE126
A	GLN273
A	PHE274
A	PHE281
A	ASN284
A	ARG340
A	ILE341
A	GLY343
A	ALA344
A	TYR345
A	MET365
A	ILE128
A	VAL366
A	SER369
A	ASN371
A	MET375
A	GRA402
A	HOH407
A	HOH418
A	HOH450
A	HOH469
A	HOH501
A	THR129
A	HOH551
B	GLN282
A	GLY134
A	SER135
A	TRP159
A	ILE160
A	SER161
A	ARG271

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GRA A 402

Chain	Residue
A	ARG87
A	ASN91
A	PHE126
A	SER135
A	VAL137
A	SER181
A	PHE239
A	ASN243
A	ARG246
A	PHE274
A	ASN315
A	VAL366
A	GLU367
A	GLY368
A	ARG385
A	ARG389
A	FAD400
A	HOH403
A	HOH440
A	HOH485
A	HOH531
A	HOH540
A	HOH552
C	LYS22
C	LYS23

---

site_id	AC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD B 400

Chain	Residue
A	GLN282
B	PHE126
B	ILE128
B	THR129
B	GLY134
B	SER135
B	TRP159
B	ILE160
B	SER161
B	LYS204
B	ARG271
B	GLN273
B	PHE274
B	PHE281
B	ASN284
B	ARG340
B	ILE341
B	GLY343
B	ALA344
B	TYR345
B	MET365
B	VAL366
B	GLU367
B	SER369
B	ASN371
B	GRA402
B	HOH409
B	HOH439

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GRA B 402

Chain	Residue
B	ARG385
B	ARG389
B	FAD400
B	HOH405
B	HOH526
D	ASP218
B	ARG87
B	ASN91
B	PHE126
B	SER135
B	VAL137
B	SER181
B	ARG236
B	PHE239
B	ASN243
B	ARG246
B	PHE274
B	ASN315
B	VAL366
B	GLU367
B	GLY368

---

site_id	AC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD C 400

Chain	Residue
C	PHE126
C	ILE128
C	THR129
C	GLY134
C	SER135
C	TRP159
C	ILE160
C	SER161
C	ARG271
C	GLN273
C	PHE274
C	ILE278
C	PHE281
C	ASN284
C	ARG340
C	ILE341
C	GLY343
C	ALA344
C	TYR345
C	MET365
C	VAL366
C	SER369
C	ASN371
C	MET375
C	GRA402
C	HOH404
C	HOH421
C	HOH430
C	HOH431
C	HOH518
C	HOH542
D	GLN282

---

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GRA C 402

Chain	Residue
A	LYS23
C	ARG87
C	ASN91
C	PHE126
C	SER135
C	VAL137
C	SER181
C	ALA235
C	PHE239
C	ASN243
C	ARG246
C	PHE274
C	ASN315
C	VAL366
C	GLU367
C	GLY368
C	ARG385
C	ARG389
C	FAD400
C	HOH407
C	HOH409
C	HOH450
C	HOH453
C	HOH491
C	HOH519

---

site_id	AC7
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD D 400

Chain	Residue
C	GLN282
D	PHE126
D	ILE128
D	THR129
D	GLY134
D	SER135
D	TRP159
D	SER161
D	ARG271
D	GLN273
D	PHE274
D	PHE281
D	ASN284
D	ARG340
D	ILE341
D	GLY343
D	ALA344
D	TYR345
D	MET365
D	VAL366
D	GLU367
D	SER369
D	ASN371
D	GRA402
D	HOH409
D	HOH413
D	HOH436
D	HOH451
D	HOH494

---

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GRA D 402

Chain	Residue
D	ARG87
D	ASN91
D	SER135
D	VAL137
D	SER181
D	PHE239
D	ASN243
D	ARG246
D	PHE274
D	ASN315
D	VAL366
D	GLU367
D	GLY368
D	ARG385
D	ARG389
D	FAD400
D	HOH424
D	HOH438
D	HOH447
D	HOH452
D	HOH462

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY127-ALA139

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	80
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20486657","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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