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3OML

Structure of full-length peroxisomal multifunctional enzyme type 2 from Drosophila melanogaster

Functional Information from GO Data
ChainGOidnamespacecontents
A0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0004303molecular_functionestradiol 17-beta-dehydrogenase [NAD(P)+] activity
A0005777cellular_componentperoxisome
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0018812molecular_function3-hydroxyacyl-CoA dehydratase activity
A0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
A0042803molecular_functionprotein homodimerization activity
A0044594molecular_function17-beta-hydroxysteroid dehydrogenase (NAD+) activity
A0106386molecular_function(3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SnsgiygnfgQvnYTAAKMGLiGLAnTVA
ChainResidueDetails
ASER154-ALA182

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. ILHGLCTLGFS
ChainResidueDetails
AILE516-SER526

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P51659, ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR167

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P51659
ChainResidueDetails
AVAL16
ALEU24
AASP43
ASER78
AASN102
ASER154
ATYR167
AALA199

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22414
ChainResidueDetails
AHIS390
ALYS419
AASP496
AGLY519
APHE549

221371

PDB entries from 2024-06-19

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