Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2IX5

Short chain specific acyl-CoA oxidase from Arabidopsis thaliana, ACX4 in complex with acetoacetyl-CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0003997	molecular_function	acyl-CoA oxidase activity
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0009514	cellular_component	glyoxysome
A	0009793	biological_process	embryo development ending in seed dormancy
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0046459	biological_process	short-chain fatty acid metabolic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	1901149	molecular_function	salicylic acid binding
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0003997	molecular_function	acyl-CoA oxidase activity
B	0005777	cellular_component	peroxisome
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0009514	cellular_component	glyoxysome
B	0009793	biological_process	embryo development ending in seed dormancy
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0046459	biological_process	short-chain fatty acid metabolic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	1901149	molecular_function	salicylic acid binding
C	0003995	molecular_function	acyl-CoA dehydrogenase activity
C	0003997	molecular_function	acyl-CoA oxidase activity
C	0005777	cellular_component	peroxisome
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0009514	cellular_component	glyoxysome
C	0009793	biological_process	embryo development ending in seed dormancy
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0046459	biological_process	short-chain fatty acid metabolic process
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	1901149	molecular_function	salicylic acid binding
D	0003995	molecular_function	acyl-CoA dehydrogenase activity
D	0003997	molecular_function	acyl-CoA oxidase activity
D	0005777	cellular_component	peroxisome
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0009514	cellular_component	glyoxysome
D	0009793	biological_process	embryo development ending in seed dormancy
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0046459	biological_process	short-chain fatty acid metabolic process
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	1901149	molecular_function	salicylic acid binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CAA A1432

Chain	Residue
A	SER181
A	LYS429
A	FAD1433
A	ALA183
A	SER184
A	PHE277
A	LEU284
A	ARG288
A	GLU408
A	GLY409
A	ARG420

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CAA B1432

Chain	Residue
B	GLY180
B	SER181
B	ALA183
B	SER184
B	PHE277
B	LEU284
B	ARG288
B	GLU408
B	GLY409
B	VAL417
B	ARG420
B	ALA426
B	LYS429
B	FAD1433
B	HOH2016
B	HOH2047
B	HOH2048

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CAA C1432

Chain	Residue
C	GLY180
C	SER181
C	ALA183
C	SER184
C	PHE277
C	LEU284
C	ARG288
C	GLU408
C	GLY409
C	ARG420
C	ALA426
C	LYS429
C	FAD1433

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CAA D1432

Chain	Residue
B	ASN200
B	GLN261
B	ASN262
D	SER181
D	ALA183
D	SER184
D	PHE277
D	ARG288
D	GLU408
D	GLY409
D	ARG420
D	ALA426
D	LYS429
D	FAD1433
D	HOH2027

site_id	AC5
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD A1433

Chain	Residue
A	VAL138
A	TRP172
A	LEU174
A	THR175
A	GLY180
A	SER181
A	TRP205
A	GLY207
A	ASN255
A	PRO403
A	THR406
A	TYR407
A	THR410
A	ASP412
A	ILE413
A	PHE428
A	CAA1432
B	ARG313
B	GLN315
B	PHE316
B	LEU320
B	PHE323
B	ASN326
B	GLU381
B	LEU382
B	GLY384
B	GLY385
D	GLN324

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD B1433

Chain	Residue
B	TRP205
B	GLY207
B	ASN255
B	PRO403
B	THR406
B	TYR407
B	THR410
B	ASP412
B	PHE428
B	CAA1432
C	GLN324
A	ARG313
A	PHE316
A	LEU320
A	PHE323
A	ASN326
A	GLU381
A	LEU382
A	GLY384
A	GLY385
B	VAL138
B	TRP172
B	LEU174
B	THR175
B	GLY180
B	SER181

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD C1433

Chain	Residue
B	GLN324
C	VAL138
C	TRP172
C	LEU174
C	THR175
C	GLY180
C	SER181
C	TRP205
C	GLY207
C	ASN255
C	PRO403
C	TYR407
C	THR410
C	ASP412
C	PHE428
C	CAA1432
C	HOH2014
D	ARG313
D	GLN315
D	PHE316
D	LEU320
D	PHE323
D	ASN326
D	GLU381
D	LEU382
D	GLY384
D	GLY385

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD D1433

Chain	Residue
A	GLN324
C	ARG313
C	PHE316
C	LEU320
C	PHE323
C	ASN326
C	GLU381
C	LEU382
C	GLY384
C	GLY385
C	HOH2042
D	TRP172
D	LEU174
D	THR175
D	GLY180
D	SER181
D	TRP205
D	GLY207
D	ASN255
D	PRO403
D	THR406
D	TYR407
D	THR410
D	ASP412
D	ILE413
D	PHE428
D	CAA1432
D	HOH2044

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA173-GLY185

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

Chain	Residue	Details
A	GLU381-ASP400

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16887802","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IX6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16887802","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IX5","evidenceCode":"ECO:0007744"}]}

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	SER287

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
B	GLN294

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
C	GLN294

site_id	CSA12
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
D	GLN294

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

Chain	Residue	Details
B	SER287

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

Chain	Residue	Details
C	SER287

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

Chain	Residue	Details
D	SER287

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

Chain	Residue	Details
A	GLU408

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

Chain	Residue	Details
B	GLU408

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

Chain	Residue	Details
C	GLU408

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

Chain	Residue	Details
D	GLU408

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1ivh

Chain	Residue	Details
A	GLN294

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