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6Z5F

CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH 3-KETODECANOYL-COA AND OXIDISED NICOTINAMIDE ADENINE DINUCLEOTIDE

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003824molecular_functioncatalytic activity
AAA0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
AAA0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
AAA0004300molecular_functionenoyl-CoA hydratase activity
AAA0005777cellular_componentperoxisome
AAA0005829cellular_componentcytosol
AAA0006631biological_processfatty acid metabolic process
AAA0006635biological_processfatty acid beta-oxidation
AAA0016491molecular_functionoxidoreductase activity
AAA0016509molecular_functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
AAA0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
AAA0016829molecular_functionlyase activity
AAA0016853molecular_functionisomerase activity
AAA0016863molecular_functionintramolecular oxidoreductase activity, transposing C=C bonds
AAA0019899molecular_functionenzyme binding
AAA0070403molecular_functionNAD+ binding
BBB0003824molecular_functioncatalytic activity
BBB0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
BBB0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
BBB0004300molecular_functionenoyl-CoA hydratase activity
BBB0005777cellular_componentperoxisome
BBB0005829cellular_componentcytosol
BBB0006631biological_processfatty acid metabolic process
BBB0006635biological_processfatty acid beta-oxidation
BBB0016491molecular_functionoxidoreductase activity
BBB0016509molecular_functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
BBB0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
BBB0016829molecular_functionlyase activity
BBB0016853molecular_functionisomerase activity
BBB0016863molecular_functionintramolecular oxidoreductase activity, transposing C=C bonds
BBB0019899molecular_functionenzyme binding
BBB0070403molecular_functionNAD+ binding
Functional Information from PROSITE/UniProt
site_idPS00067
Number of Residues25
Details3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. NcyGFVgNRmlaPYYnqgff.LLeeG
ChainResidueDetails
AAAASN474-GLY498

site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaIQGvalGGGlelaLgCHY
ChainResidueDetails
AAALEU90-TYR110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BBBGLY100
AAAGLY100

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
BBBGLU103
BBBGLU123
AAAGLU103
AAAGLU123

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Blocked amino end (Ala)
ChainResidueDetails
BBBALA2
AAAALA2

site_idSWS_FT_FI4
Number of Residues20
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBM2
ChainResidueDetails
BBBLYS38
BBBLYS182
BBBLYS241
BBBLYS253
BBBLYS279
BBBLYS289
BBBLYS330
BBBLYS531
BBBLYS576
BBBLYS721
AAALYS38
AAALYS182
AAALYS241
AAALYS253
AAALYS279
AAALYS289
AAALYS330
AAALYS531
AAALYS576
AAALYS721

site_idSWS_FT_FI5
Number of Residues14
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBM2
ChainResidueDetails
BBBLYS173
BBBLYS190
BBBLYS218
BBBLYS275
BBBLYS583
BBBLYS590
BBBLYS709
AAALYS173
AAALYS190
AAALYS218
AAALYS275
AAALYS583
AAALYS590
AAALYS709

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBM2
ChainResidueDetails
BBBLYS359
BBBLYS463
AAALYS359
AAALYS463
BBBLYS249
AAALYS249

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08426
ChainResidueDetails
BBBLYS345
AAALYS345

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08426
ChainResidueDetails
AAATHR547
BBBTHR547

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PDB entries from 2024-06-12

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