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3ZW8

Crystal Structure Of Rat Peroxisomal Multifunctional Enzyme Type 1 (rpMFE1) In Apo Form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
A0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
A0004300molecular_functionenoyl-CoA hydratase activity
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016491molecular_functionoxidoreductase activity
A0016509molecular_functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0016863molecular_functionintramolecular oxidoreductase activity, transposing C=C bonds
A0019899molecular_functionenzyme binding
A0070403molecular_functionNAD+ binding
B0003824molecular_functioncatalytic activity
B0003857molecular_function3-hydroxyacyl-CoA dehydrogenase activity
B0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
B0004300molecular_functionenoyl-CoA hydratase activity
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0016491molecular_functionoxidoreductase activity
B0016509molecular_functionlong-chain-3-hydroxyacyl-CoA dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0016863molecular_functionintramolecular oxidoreductase activity, transposing C=C bonds
B0019899molecular_functionenzyme binding
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1721
ChainResidue
AGLY72
AGLU103
AGLU123
APRO130
AGLY131
AALA132
APHE255
ASO41722

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1722
ChainResidue
AALA61
APHE66
AGLY99
AGLY100
APRO122
AGLU123
AGOL1721
AHOH2148
AGLY60

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 3001
ChainResidue
BPRO191
BILE192
BGLU193
BARG196

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1719
ChainResidue
BGLY60
BALA61
BPHE66
BGLY99
BGLY100
BGLU123

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1720
ChainResidue
ATRP594
BGLY305
BTHR306
BARG309

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1723
ChainResidue
AASN207
AASP209
ASER210
AGLY553
AASN554

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3001
ChainResidue
APRO191
AILE192
AGLU193
AARG196

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 3001
ChainResidue
BPRO191
BILE192
BGLU193
BARG196

Functional Information from PROSITE/UniProt
site_idPS00067
Number of Residues25
Details3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. NcyGFVgNRmlaPYYnqgff.LLeeG
ChainResidueDetails
AASN474-GLY498

site_idPS00166
Number of Residues21
DetailsENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaIQGvalGGGlelaLgCHY
ChainResidueDetails
ALEU90-TYR110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY100
BGLY100

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AGLU103
AGLU123
BGLU103
BGLU123

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Blocked amino end (Ala)
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI4
Number of Residues20
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBM2
ChainResidueDetails
ALYS38
ALYS721
BLYS38
BLYS182
BLYS241
BLYS253
BLYS279
BLYS289
BLYS330
BLYS531
BLYS576
ALYS182
BLYS721
ALYS241
ALYS253
ALYS279
ALYS289
ALYS330
ALYS531
ALYS576

site_idSWS_FT_FI5
Number of Residues14
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBM2
ChainResidueDetails
ALYS173
BLYS218
BLYS275
BLYS583
BLYS590
BLYS709
ALYS190
ALYS218
ALYS275
ALYS583
ALYS590
ALYS709
BLYS173
BLYS190

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBM2
ChainResidueDetails
ALYS249
ALYS359
ALYS463
BLYS249
BLYS359
BLYS463

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08426
ChainResidueDetails
ALYS345
BLYS345

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08426
ChainResidueDetails
ATHR547
BTHR547

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PDB entries from 2024-10-30

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