Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1IS2

Crystal Structure of Peroxisomal Acyl-CoA Oxidase-II from Rat Liver

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000038	biological_process	very long-chain fatty acid metabolic process
A	0003997	molecular_function	acyl-CoA oxidase activity
A	0005504	molecular_function	fatty acid binding
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005778	cellular_component	peroxisomal membrane
A	0005782	cellular_component	peroxisomal matrix
A	0006091	biological_process	generation of precursor metabolites and energy
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0006636	biological_process	unsaturated fatty acid biosynthetic process
A	0006693	biological_process	prostaglandin metabolic process
A	0007283	biological_process	spermatogenesis
A	0009062	biological_process	fatty acid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016559	biological_process	peroxisome fission
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0019395	biological_process	fatty acid oxidation
A	0030165	molecular_function	PDZ domain binding
A	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
A	0036109	biological_process	alpha-linolenic acid metabolic process
A	0042632	biological_process	cholesterol homeostasis
A	0042759	biological_process	long-chain fatty acid biosynthetic process
A	0042803	molecular_function	protein homodimerization activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050665	biological_process	hydrogen peroxide biosynthetic process
A	0055088	biological_process	lipid homeostasis
A	0071949	molecular_function	FAD binding
A	0120524	molecular_function	long-chain fatty acyl-CoA oxidase activity
A	0140493	biological_process	very long-chain fatty acid beta-oxidation
A	1901570	biological_process	fatty acid derivative biosynthetic process
B	0000038	biological_process	very long-chain fatty acid metabolic process
B	0003997	molecular_function	acyl-CoA oxidase activity
B	0005504	molecular_function	fatty acid binding
B	0005737	cellular_component	cytoplasm
B	0005777	cellular_component	peroxisome
B	0005778	cellular_component	peroxisomal membrane
B	0005782	cellular_component	peroxisomal matrix
B	0006091	biological_process	generation of precursor metabolites and energy
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0006636	biological_process	unsaturated fatty acid biosynthetic process
B	0006693	biological_process	prostaglandin metabolic process
B	0007283	biological_process	spermatogenesis
B	0009062	biological_process	fatty acid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016559	biological_process	peroxisome fission
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0019395	biological_process	fatty acid oxidation
B	0030165	molecular_function	PDZ domain binding
B	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
B	0036109	biological_process	alpha-linolenic acid metabolic process
B	0042632	biological_process	cholesterol homeostasis
B	0042759	biological_process	long-chain fatty acid biosynthetic process
B	0042803	molecular_function	protein homodimerization activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050665	biological_process	hydrogen peroxide biosynthetic process
B	0055088	biological_process	lipid homeostasis
B	0071949	molecular_function	FAD binding
B	0120524	molecular_function	long-chain fatty acyl-CoA oxidase activity
B	0140493	biological_process	very long-chain fatty acid beta-oxidation
B	1901570	biological_process	fatty acid derivative biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD A 699

Chain	Residue
A	LEU102
A	PHE420
A	GLU423
A	THR425
A	VAL426
A	HOH1029
A	HOH1304
A	HOH1375
B	ARG307
B	GLN309
B	SER310
A	THR139
B	PHE324
B	THR326
B	GLN327
B	LYS330
B	ALA395
B	GLY397
B	GLY398
B	TYR401
A	GLY144
A	THR145
A	TRP176
A	PRO177
A	GLY178
A	PRO416
A	THR419

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD B 1699

Chain	Residue
A	ARG307
A	SER310
A	PHE324
A	THR326
A	GLN327
A	LYS330
A	ALA395
A	GLY397
A	GLY398
A	TYR401
A	HOH1033
A	HOH1066
B	LEU102
B	THR139
B	GLY144
B	THR145
B	TRP176
B	GLY178
B	ASN237
B	PRO416
B	THR419
B	GLU423
B	THR425

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	11
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pl.SNkLTYGTM

Chain	Residue	Details
A	PRO268-MET278

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11872165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16672280","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11872165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16672280","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q15067","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	7
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9R0H0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9R0H0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q15067","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9R0H0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R0H0","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	VAL281

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

Chain	Residue	Details
B	VAL281

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

Chain	Residue	Details
A	GLU421

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

Chain	Residue	Details
B	GLU421

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

Chain	Residue	Details
A	PHE284

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

Chain	Residue	Details
B	PHE284

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

Chain	Residue	Details
A	GLY276

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)