5MGB
Crystal Structure of Rat Peroxisomal Multifunctional enzyme Type-1 (RPMFE1) Complexed with Acetoacetyl-CoA and NAD
Replaces: 5AAKFunctional 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 | 4 |
| Details | binding site for residue SO4 A 801 |
| Chain | Residue |
| A | PRO191 |
| A | ILE192 |
| A | GLU193 |
| A | ARG196 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 802 |
| Chain | Residue |
| A | GLY262 |
| A | HOH938 |
| 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 | 14 |
| Details | binding site for residue CAA A 804 |
| Chain | Residue |
| A | ALA59 |
| A | GLY60 |
| A | ALA61 |
| A | ASP62 |
| A | ILE63 |
| A | PHE66 |
| A | GLY100 |
| A | GLU103 |
| A | ARG118 |
| A | GLU123 |
| A | TYR156 |
| B | LYS249 |
| A | PRO20 |
| A | VAL21 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue NAD A 805 |
| Chain | Residue |
| A | LEU302 |
| A | GLY303 |
| A | GLY305 |
| A | THR306 |
| A | MET307 |
| A | GLU326 |
| A | SER327 |
| A | GLN331 |
| A | ALA380 |
| A | VAL381 |
| A | PHE382 |
| A | GLU383 |
| A | LYS388 |
| A | VAL391 |
| A | ASN408 |
| A | SER410 |
| A | HIS431 |
| A | PHE432 |
| A | SER434 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 806 |
| Chain | Residue |
| A | LYS265 |
| A | PHE664 |
| A | ALA667 |
| A | SER668 |
| A | PRO707 |
| A | LEU708 |
| A | HOH924 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 807 |
| Chain | Residue |
| A | PRO548 |
| A | ARG550 |
| A | HIS606 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 801 |
| Chain | Residue |
| B | PRO191 |
| B | ILE192 |
| B | GLU193 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for residue CAA B 802 |
| Chain | Residue |
| B | PRO20 |
| B | VAL21 |
| B | ALA59 |
| B | GLY60 |
| B | ALA61 |
| B | ASP62 |
| B | ILE63 |
| B | PHE66 |
| B | LEU75 |
| B | GLY100 |
| B | GLU103 |
| B | PRO122 |
| B | GLU123 |
| B | GLY131 |
| B | TYR156 |
| B | LYS275 |
| B | LYS463 |
| site_id | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue NAD B 803 |
| Chain | Residue |
| A | THR597 |
| B | LEU302 |
| B | GLY303 |
| B | GLY305 |
| B | THR306 |
| B | MET307 |
| B | GLU326 |
| B | SER327 |
| B | GLN331 |
| B | VAL381 |
| B | PHE382 |
| B | GLU383 |
| B | LYS388 |
| B | VAL391 |
| B | ASN408 |
| B | SER410 |
| B | HIS431 |
| B | PHE432 |
| B | SER434 |
| B | HOH905 |
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 | LYS721 | |
| B | LYS38 | |
| B | LYS182 | |
| B | LYS241 | |
| B | LYS253 | |
| B | LYS279 | |
| B | LYS289 | |
| B | LYS330 | |
| B | LYS531 | |
| B | LYS576 | |
| A | LYS182 | |
| B | LYS721 | |
| A | LYS241 | |
| A | LYS253 | |
| A | LYS279 | |
| A | LYS289 | |
| A | LYS330 | |
| A | LYS531 | |
| A | LYS576 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBM2 |
| Chain | Residue | Details |
| A | LYS173 | |
| B | LYS218 | |
| B | LYS275 | |
| B | LYS583 | |
| B | LYS590 | |
| B | LYS709 | |
| A | LYS190 | |
| A | LYS218 | |
| A | LYS275 | |
| A | LYS583 | |
| A | LYS590 | |
| A | LYS709 | |
| B | LYS173 | |
| B | LYS190 |
| 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 |
