Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1RX0

Crystal structure of isobutyryl-CoA dehydrogenase complexed with substrate/ligand.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003853	molecular_function	short-chain 2-methyl fatty acyl-CoA dehydrogenase activity
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006351	biological_process	DNA-templated transcription
A	0006574	biological_process	L-valine catabolic process
A	0006629	biological_process	lipid metabolic process
A	0009083	biological_process	branched-chain amino acid catabolic process
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	0003853	molecular_function	short-chain 2-methyl fatty acyl-CoA dehydrogenase activity
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006351	biological_process	DNA-templated transcription
B	0006574	biological_process	L-valine catabolic process
B	0006629	biological_process	lipid metabolic process
B	0009083	biological_process	branched-chain amino acid catabolic process
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	0003853	molecular_function	short-chain 2-methyl fatty acyl-CoA dehydrogenase activity
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006351	biological_process	DNA-templated transcription
C	0006574	biological_process	L-valine catabolic process
C	0006629	biological_process	lipid metabolic process
C	0009083	biological_process	branched-chain amino acid catabolic process
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	0003853	molecular_function	short-chain 2-methyl fatty acyl-CoA dehydrogenase activity
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006351	biological_process	DNA-templated transcription
D	0006574	biological_process	L-valine catabolic process
D	0006629	biological_process	lipid metabolic process
D	0009083	biological_process	branched-chain amino acid catabolic process
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	1
Details	BINDING SITE FOR RESIDUE EDO A 2001

Chain	Residue
A	HOH9289

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO C 2002

Chain	Residue
C	PHE31

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 2003

Chain	Residue
B	PHE169
B	GLU211
B	HOH9370
D	TYR354
D	LEU357
D	HOH9255
D	HOH9339

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 2004

Chain	Residue
B	ILE193
B	PHE244
B	ALA247

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 2005

Chain	Residue
C	ARG249
C	GLU321
C	ARG322
C	HOH9149

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 2006

Chain	Residue
B	PRO15

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 2007

Chain	Residue
B	HIS276
B	TYR360
B	HOH9021
B	HOH9391

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 2008

Chain	Residue
A	PRO141
C	TYR354
C	TYR360

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO D 2009

Chain	Residue
D	THR92

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 2010

Chain	Residue
B	HOH9319
D	PHE283
D	GLY284
D	HOH9254

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 2011

Chain	Residue
A	LYS156
A	ARG236
A	HOH9009

site_id	BC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD A 399

Chain	Residue
A	TYR136
A	LEU138
A	THR139
A	GLY144
A	SER145
A	PHE169
A	ILE170
A	SER171
A	TRP216
A	VAL371
A	LEU375
A	SER378
A	GLU380
A	HOH9118
A	HOH9123
A	HOH9209
A	HOH9210
B	GLN291
C	ARG280
C	PHE283
C	ASN290
C	LEU293
C	GLN349
C	MET350
C	GLY353
C	TYR354
C	HOH9082
C	HOH9083

site_id	BC4
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD B 399

Chain	Residue
A	GLN291
B	TYR136
B	LEU138
B	THR139
B	GLY144
B	SER145
B	PHE169
B	ILE170
B	SER171
B	TRP216
B	VAL371
B	LEU375
B	SER378
B	GLU380
B	HOH9326
B	HOH9381
B	HOH9402
D	ARG280
D	PHE283
D	ASN290
D	LEU293
D	GLN349
D	MET350
D	GLY352
D	GLY353
D	TYR354
D	ACY9002
D	HOH9273
D	HOH9274

site_id	BC5
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD C 399

Chain	Residue
C	TYR136
C	LEU138
C	THR139
C	GLY144
C	SER145
C	PHE169
C	ILE170
C	SER171
C	VAL371
C	LEU375
C	SER378
C	GLU380
C	2MC400
C	HOH9137
C	HOH9270
C	HOH9271
C	HOH9329
D	GLN291
A	ARG280
A	PHE283
A	ASN290
A	LEU293
A	GLN349
A	MET350
A	GLY352
A	GLY353
A	TYR354
A	HOH9361

site_id	BC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD D 399

Chain	Residue
B	ARG280
B	PHE283
B	ASN290
B	LEU293
B	GLN349
B	MET350
B	GLY352
B	GLY353
B	TYR354
B	ACY9001
B	HOH9390
C	GLN291
D	TYR136
D	LEU138
D	THR139
D	GLY144
D	SER145
D	PHE169
D	ILE170
D	SER171
D	VAL371
D	ILE374
D	LEU375
D	SER378
D	GLU380
D	2MC400
D	HOH9334
D	HOH9346
D	HOH9347

site_id	BC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE 2MC C 400

Chain	Residue
C	ILE103
C	TYR136
C	THR139
C	SER145
C	ALA147
C	PHE244
C	VAL248
C	LEU251
C	ASN252
C	ARG255
C	VAL326
C	LEU375
C	GLU376
C	GLY377
C	LEU385
C	ARG388
C	FAD399
C	HOH9202
C	HOH9203
C	HOH9269
C	HOH9349
C	HOH9350

site_id	BC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 2MC D 400

Chain	Residue
D	ILE103
D	TYR136
D	THR139
D	SER145
D	ALA147
D	PHE244
D	VAL248
D	LEU251
D	ASN252
D	ARG255
D	VAL326
D	LEU375
D	GLU376
D	GLY377
D	LEU385
D	ARG388
D	FAD399
D	HOH9128
D	HOH9129
D	HOH9130
D	HOH9333

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY B 9001

Chain	Residue
B	HOH9141
D	FAD399

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACY D 9002

Chain	Residue
B	FAD399

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY D 9003

Chain	Residue
D	LEU62
D	PHE64

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY C 9004

Chain	Residue
C	GLY142
C	SER143
C	SER149
C	HOH9267

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY A 9005

Chain	Residue
A	TYR68
A	LEU78
A	ARG80
A	TRP109
A	HOH9088
A	HOH9089
A	HOH9090

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY B 9006

Chain	Residue
B	GLN61
B	LEU62
B	GLY63
B	HOH9118

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY D 9007

Chain	Residue
D	ARG312
D	HOH9312

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS137-SER149

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14752098","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	52
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"14752098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14752098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D7B6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D7B6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D7B6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
A	GLY254

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
B	GLY254

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
C	GLY254

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
D	GLY254

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
A	GLU376

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
B	GLU376

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
C	GLU376

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
D	GLU376

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