5OMO
CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH WITH 3S-HYDROXY-DECANOYL-COA AND 3-KETO-DECANOYL-COA
Replaces: 5AAJFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
| A | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016509 | molecular_function | long-chain-3-hydroxyacyl-CoA dehydrogenase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016863 | molecular_function | intramolecular oxidoreductase activity, transposing C=C bonds |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
| B | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016509 | molecular_function | long-chain-3-hydroxyacyl-CoA dehydrogenase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016863 | molecular_function | intramolecular oxidoreductase activity, transposing C=C bonds |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 801 |
| Chain | Residue |
| A | PRO191 |
| A | ILE192 |
| A | GLU193 |
| A | ARG196 |
| A | HOH917 |
| A | HOH924 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 802 |
| Chain | Residue |
| A | ARG220 |
| A | HOH1013 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 803 |
| Chain | Residue |
| A | ARG641 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 804 |
| Chain | Residue |
| A | PRO548 |
| A | VAL549 |
| A | ARG550 |
| A | HIS606 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 805 |
| Chain | Residue |
| A | SER261 |
| A | GLY262 |
| A | GLN263 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for residue HSC A 806 |
| Chain | Residue |
| A | PRO20 |
| A | VAL21 |
| A | ALA23 |
| A | VAL24 |
| A | PRO26 |
| A | ILE29 |
| A | ALA59 |
| A | GLY60 |
| A | ALA61 |
| A | ASP62 |
| A | ILE63 |
| A | PHE66 |
| A | GLY72 |
| A | GLY100 |
| A | GLU103 |
| A | PRO122 |
| A | GLU123 |
| A | LEU126 |
| A | GLY131 |
| A | TYR156 |
| A | PHE255 |
| A | LYS275 |
| B | LYS249 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue ZOZ A 807 |
| Chain | Residue |
| A | SER410 |
| A | HIS431 |
| A | SER434 |
| A | PRO435 |
| A | ASN481 |
| A | LYS514 |
| A | MET515 |
| A | VAL520 |
| A | GLY652 |
| A | HOH997 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 801 |
| Chain | Residue |
| A | TRP594 |
| B | GLY305 |
| B | THR306 |
| B | ARG309 |
| B | HOH918 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 802 |
| Chain | Residue |
| B | ILE192 |
| B | GLU193 |
| B | ARG196 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 803 |
| Chain | Residue |
| B | TYR488 |
| B | PHE492 |
| B | SER521 |
| B | ARG533 |
| B | HOH915 |
| B | HOH928 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 804 |
| Chain | Residue |
| A | GLN94 |
| A | ASN114 |
| A | ASP175 |
| B | SER67 |
| B | PHE69 |
| B | THR70 |
| site_id | AD3 |
| Number of Residues | 22 |
| Details | binding site for residue HSC B 805 |
| Chain | Residue |
| B | PRO20 |
| B | ALA59 |
| B | GLY60 |
| B | ALA61 |
| B | ASP62 |
| B | ILE63 |
| B | VAL96 |
| B | LEU98 |
| B | GLY100 |
| B | GLU103 |
| B | PRO122 |
| B | GLU123 |
| B | LEU126 |
| B | PRO130 |
| B | GLY131 |
| B | TYR156 |
| B | PHE255 |
| B | PHE271 |
| B | PHE272 |
| B | LYS275 |
| B | LYS279 |
| B | HOH950 |
Functional Information from PROSITE/UniProt
| site_id | PS00067 |
| Number of Residues | 25 |
| Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. NcyGFVgNRmlaPYYnqgff.LLeeG |
| Chain | Residue | Details |
| A | ASN474-GLY498 |
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaIQGvalGGGlelaLgCHY |
| Chain | Residue | Details |
| A | LEU90-TYR110 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY100 | |
| B | GLY100 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU103 | |
| A | GLU123 | |
| B | GLU103 | |
| B | GLU123 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Blocked amino end (Ala) |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBM2 |
| Chain | Residue | Details |
| A | LYS38 | |
| A | LYS182 | |
| A | LYS241 | |
| A | LYS253 | |
| A | LYS279 | |
| A | LYS289 | |
| A | LYS330 | |
| A | LYS531 | |
| A | LYS576 | |
| A | LYS721 | |
| B | LYS38 | |
| B | LYS182 | |
| B | LYS241 | |
| B | LYS253 | |
| B | LYS279 | |
| B | LYS289 | |
| B | LYS330 | |
| B | LYS531 | |
| B | LYS576 | |
| B | LYS721 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBM2 |
| Chain | Residue | Details |
| A | LYS173 | |
| A | LYS190 | |
| A | LYS218 | |
| A | LYS275 | |
| A | LYS583 | |
| A | LYS590 | |
| A | LYS709 | |
| B | LYS173 | |
| B | LYS190 | |
| B | LYS218 | |
| B | LYS275 | |
| B | LYS583 | |
| B | LYS590 | |
| B | LYS709 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBM2 |
| Chain | Residue | Details |
| A | LYS249 | |
| A | LYS359 | |
| A | LYS463 | |
| B | LYS249 | |
| B | LYS359 | |
| B | LYS463 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08426 |
| Chain | Residue | Details |
| A | LYS345 | |
| B | LYS345 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08426 |
| Chain | Residue | Details |
| A | THR547 | |
| B | THR547 |
