Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5K3I

Crystal structure of Acyl-CoA oxidase-1 in Caenorhabditis elegans complexed with FAD and ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
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	0071949	molecular_function	FAD binding
A	1904070	biological_process	ascaroside biosynthetic process
B	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
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	0071949	molecular_function	FAD binding
B	1904070	biological_process	ascaroside biosynthetic process
C	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
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	0071949	molecular_function	FAD binding
C	1904070	biological_process	ascaroside biosynthetic process
D	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
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	0071949	molecular_function	FAD binding
D	1904070	biological_process	ascaroside biosynthetic process
E	0000166	molecular_function	nucleotide binding
E	0003997	molecular_function	acyl-CoA oxidase activity
E	0005504	molecular_function	fatty acid binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005777	cellular_component	peroxisome
E	0005782	cellular_component	peroxisomal matrix
E	0006629	biological_process	lipid metabolic process
E	0006631	biological_process	fatty acid metabolic process
E	0006635	biological_process	fatty acid beta-oxidation
E	0016491	molecular_function	oxidoreductase activity
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
E	0042811	biological_process	pheromone biosynthetic process
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0071949	molecular_function	FAD binding
E	1904070	biological_process	ascaroside biosynthetic process
F	0000166	molecular_function	nucleotide binding
F	0003997	molecular_function	acyl-CoA oxidase activity
F	0005504	molecular_function	fatty acid binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005777	cellular_component	peroxisome
F	0005782	cellular_component	peroxisomal matrix
F	0006629	biological_process	lipid metabolic process
F	0006631	biological_process	fatty acid metabolic process
F	0006635	biological_process	fatty acid beta-oxidation
F	0016491	molecular_function	oxidoreductase activity
F	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
F	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
F	0042811	biological_process	pheromone biosynthetic process
F	0050660	molecular_function	flavin adenine dinucleotide binding
F	0071949	molecular_function	FAD binding
F	1904070	biological_process	ascaroside biosynthetic process
G	0000166	molecular_function	nucleotide binding
G	0003997	molecular_function	acyl-CoA oxidase activity
G	0005504	molecular_function	fatty acid binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005777	cellular_component	peroxisome
G	0005782	cellular_component	peroxisomal matrix
G	0006629	biological_process	lipid metabolic process
G	0006631	biological_process	fatty acid metabolic process
G	0006635	biological_process	fatty acid beta-oxidation
G	0016491	molecular_function	oxidoreductase activity
G	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
G	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
G	0042811	biological_process	pheromone biosynthetic process
G	0050660	molecular_function	flavin adenine dinucleotide binding
G	0071949	molecular_function	FAD binding
G	1904070	biological_process	ascaroside biosynthetic process
H	0000166	molecular_function	nucleotide binding
H	0003997	molecular_function	acyl-CoA oxidase activity
H	0005504	molecular_function	fatty acid binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005777	cellular_component	peroxisome
H	0005782	cellular_component	peroxisomal matrix
H	0006629	biological_process	lipid metabolic process
H	0006631	biological_process	fatty acid metabolic process
H	0006635	biological_process	fatty acid beta-oxidation
H	0016491	molecular_function	oxidoreductase activity
H	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
H	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
H	0042811	biological_process	pheromone biosynthetic process
H	0050660	molecular_function	flavin adenine dinucleotide binding
H	0071949	molecular_function	FAD binding
H	1904070	biological_process	ascaroside biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue FAD A 701

Chain	Residue
A	LEU115
A	THR432
A	GLU436
A	MET438
A	VAL439
B	ARG320
B	GLN322
B	VAL334
B	TYR337
B	THR339
B	GLN340
A	TYR149
B	ARG343
B	ALA408
B	GLY410
B	GLY411
B	TYR414
B	HOH803
A	GLN151
A	THR152
A	GLY157
A	THR158
A	TRP189
A	PRO190
A	GLY191

site_id	AC2
Number of Residues	16
Details	binding site for residue ATP A 702

Chain	Residue
A	SER392
A	HIS396
A	ASN437
A	MET438
A	ARG533
A	ARG536
A	TYR581
A	HOH839
A	HOH847
A	HOH848
B	HIS342
B	ARG343
B	GLN404
B	TYR573
B	MG701
B	HOH814

site_id	AC3
Number of Residues	2
Details	binding site for residue MG A 703

Chain	Residue
A	ASP577
B	ATP703

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 701

Chain	Residue
A	ATP702
A	HOH839
B	ASP577

site_id	AC5
Number of Residues	24
Details	binding site for residue FAD B 702

Chain	Residue
A	ARG320
A	GLN322
A	VAL334
A	TYR337
A	THR339
A	GLN340
A	ARG343
A	ALA408
A	GLY410
A	GLY411
A	TYR414
B	LEU115
B	TYR149
B	GLN151
B	THR152
B	GLY157
B	THR158
B	TRP189
B	GLY191
B	THR432
B	GLU436
B	MET438
B	VAL439
B	HOH807

site_id	AC6
Number of Residues	14
Details	binding site for residue ATP B 703

Chain	Residue
A	HIS342
A	ARG343
A	GLN404
A	TYR573
A	MG703
B	SER392
B	HIS396
B	ASN437
B	MET438
B	LEU441
B	ARG533
B	ARG536
B	TYR581
B	HOH864

site_id	AC7
Number of Residues	27
Details	binding site for residue FAD C 701

Chain	Residue
C	HOH824
C	HOH848
D	ARG320
D	GLN322
D	VAL334
D	TYR337
D	GLN340
D	ARG343
D	ALA408
D	GLY410
D	GLY411
D	TYR414
C	LEU115
C	TYR149
C	GLN151
C	THR152
C	GLY157
C	THR158
C	TRP189
C	PRO190
C	GLY191
C	THR432
C	GLU436
C	MET438
C	VAL439
C	HOH806
C	HOH821

site_id	AC8
Number of Residues	3
Details	binding site for residue MG C 702

Chain	Residue
C	ASP577
D	ATP801
D	HOH935

site_id	AC9
Number of Residues	15
Details	binding site for residue ATP C 703

Chain	Residue
C	SER392
C	HIS396
C	ASN437
C	MET438
C	LEU441
C	ARG533
C	ARG536
C	TYR581
C	HOH811
D	HIS342
D	ARG343
D	GLN404
D	TYR573
D	MG802
D	HOH916

site_id	AD1
Number of Residues	14
Details	binding site for residue ATP D 801

Chain	Residue
C	HIS342
C	GLN404
C	TYR573
C	MG702
D	SER392
D	HIS396
D	ASN437
D	MET438
D	LEU441
D	ARG533
D	ARG536
D	TYR581
D	HOH931
D	HOH935

site_id	AD2
Number of Residues	2
Details	binding site for residue MG D 802

Chain	Residue
C	ARG533
C	ATP703

site_id	AD3
Number of Residues	25
Details	binding site for residue FAD D 803

Chain	Residue
C	ARG320
C	GLN322
C	VAL334
C	TYR337
C	THR339
C	GLN340
C	ARG343
C	ALA408
C	GLY410
C	GLY411
D	LEU115
D	TYR149
D	GLN151
D	THR152
D	GLY157
D	THR158
D	TRP189
D	PRO190
D	GLY191
D	THR432
D	TYR433
D	GLU436
D	MET438
D	VAL439
D	HOH903

site_id	AD4
Number of Residues	24
Details	binding site for residue FAD E 701

Chain	Residue
E	LEU115
E	TYR149
E	GLN151
E	THR152
E	GLY157
E	THR158
E	TRP189
E	PRO190
E	GLY191
E	THR432
E	GLU436
E	MET438
E	VAL439
F	ARG320
F	GLN322
F	VAL334
F	TYR337
F	GLN340
F	ARG343
F	ALA408
F	GLY410
F	GLY411
F	TYR414
F	HOH804

site_id	AD5
Number of Residues	3
Details	binding site for residue MG E 702

Chain	Residue
E	ASP577
E	HOH839
F	ATP702

site_id	AD6
Number of Residues	15
Details	binding site for residue ATP E 703

Chain	Residue
E	SER392
E	HIS396
E	ASN437
E	MET438
E	ARG533
E	ARG536
E	TYR581
E	HOH801
E	HOH823
E	HOH828
F	HIS342
F	ARG343
F	GLN404
F	TYR573
F	MG703

site_id	AD7
Number of Residues	23
Details	binding site for residue FAD F 701

Chain	Residue
E	ARG320
E	GLN322
E	VAL334
E	TYR337
E	GLN340
E	ARG343
E	ALA408
E	GLY410
E	GLY411
E	TYR414
E	HOH826
F	LEU115
F	TYR149
F	GLN151
F	THR152
F	GLY157
F	THR158
F	TRP189
F	THR432
F	GLU436
F	MET438
F	VAL439
F	HOH803

site_id	AD8
Number of Residues	11
Details	binding site for residue ATP F 702

Chain	Residue
E	HIS342
E	GLN404
E	TYR573
E	MG702
F	SER392
F	HIS396
F	ASN437
F	MET438
F	ARG533
F	ARG536
F	TYR581

site_id	AD9
Number of Residues	2
Details	binding site for residue MG F 703

Chain	Residue
E	ATP703
F	ASP577

site_id	AE1
Number of Residues	24
Details	binding site for residue FAD G 701

Chain	Residue
G	LEU115
G	TYR149
G	GLN151
G	THR152
G	GLY157
G	THR158
G	TRP189
G	PRO190
G	GLY191
G	THR432
G	GLU436
G	MET438
G	VAL439
G	HOH819
H	ARG320
H	GLN322
H	VAL334
H	TYR337
H	GLN340
H	ARG343
H	ALA408
H	GLY410
H	GLY411
H	TYR414

site_id	AE2
Number of Residues	2
Details	binding site for residue MG G 702

Chain	Residue
G	ASP577
H	ATP702

site_id	AE3
Number of Residues	13
Details	binding site for residue ATP G 703

Chain	Residue
G	SER392
G	HIS396
G	ASN437
G	MET438
G	LEU441
G	ARG533
G	ARG536
G	TYR581
H	HIS342
H	ARG343
H	GLN404
H	TYR573
H	MG703

site_id	AE4
Number of Residues	29
Details	binding site for residue FAD H 701

Chain	Residue
G	ARG320
G	GLN322
G	VAL334
G	TYR337
G	THR339
G	GLN340
G	ARG343
G	ALA408
G	GLY410
G	GLY411
G	TYR414
G	HOH837
H	LEU115
H	TYR149
H	GLN151
H	THR152
H	GLY157
H	THR158
H	TRP189
H	PRO190
H	GLY191
H	THR432
H	GLU436
H	MET438
H	VAL439
H	HOH803
H	HOH835
H	HOH849
H	HOH858

site_id	AE5
Number of Residues	12
Details	binding site for residue ATP H 702

Chain	Residue
G	HIS342
G	ARG343
G	GLN404
G	TYR573
G	MG702
H	SER392
H	HIS396
H	ASN437
H	MET438
H	ARG533
H	ARG536
H	TYR581

site_id	AE6
Number of Residues	2
Details	binding site for residue MG H 703

Chain	Residue
G	ATP703
H	ASP577

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PIRSR","id":"PIRSR000168-1","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	80
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"27551084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5K3I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PIRSR","id":"PIRSR000168-2","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27551084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5K3I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O62137","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27551084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5K3I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"O62137","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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