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5K3G

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003997molecular_functionacyl-CoA oxidase activity
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
A0042811biological_processpheromone biosynthetic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
A1904070biological_processascaroside biosynthetic process
B0000166molecular_functionnucleotide binding
B0003997molecular_functionacyl-CoA oxidase activity
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
B0042811biological_processpheromone biosynthetic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0071949molecular_functionFAD binding
B1904070biological_processascaroside biosynthetic process
C0000166molecular_functionnucleotide binding
C0003997molecular_functionacyl-CoA oxidase activity
C0005504molecular_functionfatty acid binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005777cellular_componentperoxisome
C0005782cellular_componentperoxisomal matrix
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006635biological_processfatty acid beta-oxidation
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
C0042811biological_processpheromone biosynthetic process
C0050660molecular_functionflavin adenine dinucleotide binding
C0071949molecular_functionFAD binding
C1904070biological_processascaroside biosynthetic process
D0000166molecular_functionnucleotide binding
D0003997molecular_functionacyl-CoA oxidase activity
D0005504molecular_functionfatty acid binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005777cellular_componentperoxisome
D0005782cellular_componentperoxisomal matrix
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006635biological_processfatty acid beta-oxidation
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
D0042811biological_processpheromone biosynthetic process
D0050660molecular_functionflavin adenine dinucleotide binding
D0071949molecular_functionFAD binding
D1904070biological_processascaroside biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"27551084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5K3I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27551084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5K3I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O62137","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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