Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5K3G

Crystals structure of Acyl-CoA oxidase-1 in Caenorhabditis elegans, Apo form-I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003997	molecular_function	acyl-CoA oxidase activity
A	0005504	molecular_function	fatty acid binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0009058	biological_process	biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
A	0042811	biological_process	pheromone biosynthetic process
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0055088	biological_process	lipid homeostasis
A	0071949	molecular_function	FAD binding
A	1904070	biological_process	ascaroside biosynthetic process
B	0003997	molecular_function	acyl-CoA oxidase activity
B	0005504	molecular_function	fatty acid binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005777	cellular_component	peroxisome
B	0005782	cellular_component	peroxisomal matrix
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0009058	biological_process	biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
B	0042811	biological_process	pheromone biosynthetic process
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0055088	biological_process	lipid homeostasis
B	0071949	molecular_function	FAD binding
B	1904070	biological_process	ascaroside biosynthetic process
C	0003997	molecular_function	acyl-CoA oxidase activity
C	0005504	molecular_function	fatty acid binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005777	cellular_component	peroxisome
C	0005782	cellular_component	peroxisomal matrix
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0009058	biological_process	biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
C	0042811	biological_process	pheromone biosynthetic process
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0055088	biological_process	lipid homeostasis
C	0071949	molecular_function	FAD binding
C	1904070	biological_process	ascaroside biosynthetic process
D	0003997	molecular_function	acyl-CoA oxidase activity
D	0005504	molecular_function	fatty acid binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005777	cellular_component	peroxisome
D	0005782	cellular_component	peroxisomal matrix
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0009058	biological_process	biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
D	0042811	biological_process	pheromone biosynthetic process
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0055088	biological_process	lipid homeostasis
D	0071949	molecular_function	FAD binding
D	1904070	biological_process	ascaroside biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PIRSR:PIRSR000168-1

Chain	Residue	Details
A	GLU434
B	GLU434
C	GLU434
D	GLU434

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: in other chain => ECO:0000269\|PubMed:27551084, ECO:0007744\|PDB:5K3I

Chain	Residue	Details
A	TYR149
B	HIS396
B	ARG533
B	TYR581
C	TYR149
C	GLY157
C	SER392
C	HIS396
C	ARG533
C	TYR581
D	TYR149
A	GLY157
D	GLY157
D	SER392
D	HIS396
D	ARG533
D	TYR581
A	SER392
A	HIS396
A	ARG533
A	TYR581
B	TYR149
B	GLY157
B	SER392

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: in other chain => ECO:0000255\|PIRSR:PIRSR000168-2, ECO:0000269\|PubMed:27551084, ECO:0007744\|PDB:5K3I

Chain	Residue	Details
A	GLY191
B	GLY191
C	GLY191
D	GLY191

site_id	SWS_FT_FI4
Number of Residues	20
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:O62137

Chain	Residue	Details
A	LYS285
B	TYR433
C	LYS285
C	ARG295
C	HIS342
C	GLY411
C	TYR433
D	LYS285
D	ARG295
D	HIS342
D	GLY411
A	ARG295
D	TYR433
A	HIS342
A	GLY411
A	TYR433
B	LYS285
B	ARG295
B	HIS342
B	GLY411

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:27551084, ECO:0007744\|PDB:5K3I

Chain	Residue	Details
A	ARG320
D	ARG320
D	GLN340
D	GLN404
A	GLN340
A	GLN404
B	ARG320
B	GLN340
B	GLN404
C	ARG320
C	GLN340
C	GLN404

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: in other chain => ECO:0000250\|UniProtKB:O62137

Chain	Residue	Details
A	GLU436
B	GLU436
C	GLU436
D	GLU436

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