2X58
The crystal structure of MFE1 liganded with CoA
Functional 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 | 12 |
| Details | BINDING SITE FOR RESIDUE ADP A 750 |
| Chain | Residue |
| A | LEU302 |
| A | VAL381 |
| A | LEU387 |
| A | HOH2100 |
| A | GLY303 |
| A | GLY305 |
| A | THR306 |
| A | MET307 |
| A | GLU326 |
| A | SER327 |
| A | GLN331 |
| A | ALA380 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE COA A 760 |
| Chain | Residue |
| A | PRO20 |
| A | VAL21 |
| A | ALA23 |
| A | ALA59 |
| A | ALA61 |
| A | ASP62 |
| A | ILE63 |
| A | HIS64 |
| A | ARG118 |
| A | GLU123 |
| A | TYR156 |
| A | GOL770 |
| B | LYS249 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 770 |
| Chain | Residue |
| A | GLU103 |
| A | GLU123 |
| A | PRO130 |
| A | GLY131 |
| A | ALA132 |
| A | PHE255 |
| A | COA760 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE COA B 760 |
| Chain | Residue |
| B | PRO20 |
| B | ALA59 |
| B | ALA61 |
| B | ASP62 |
| B | ILE63 |
| B | VAL96 |
| B | GLY99 |
| B | TYR156 |
| B | LYS275 |
| B | LYS279 |
| B | GOL770 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 770 |
| Chain | Residue |
| B | LEU73 |
| B | GLU103 |
| B | GLU123 |
| B | PRO130 |
| B | GLY131 |
| B | ALA132 |
| B | COA760 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 780 |
| Chain | Residue |
| B | VAL549 |
| B | ARG550 |
| B | HIS606 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1721 |
| Chain | Residue |
| A | PRO191 |
| A | ILE192 |
| A | GLU193 |
| A | ARG196 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1719 |
| Chain | Residue |
| B | GLY305 |
| B | THR306 |
| B | MET307 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1722 |
| Chain | Residue |
| A | GLY40 |
| A | TYR85 |
| A | GLN86 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1723 |
| Chain | Residue |
| A | TYR257 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1720 |
| Chain | Residue |
| B | PRO191 |
| B | ILE192 |
| B | GLU193 |
| B | ARG196 |
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 |
