3ZW8
Crystal Structure Of Rat Peroxisomal Multifunctional Enzyme Type 1 (rpMFE1) In Apo Form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) 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 | 0005782 | cellular_component | peroxisomal matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016509 | molecular_function | long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) 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 | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) 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 | 0005782 | cellular_component | peroxisomal matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016509 | molecular_function | long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) 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 | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1721 |
| Chain | Residue |
| A | GLY72 |
| A | GLU103 |
| A | GLU123 |
| A | PRO130 |
| A | GLY131 |
| A | ALA132 |
| A | PHE255 |
| A | SO41722 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1722 |
| Chain | Residue |
| A | ALA61 |
| A | PHE66 |
| A | GLY99 |
| A | GLY100 |
| A | PRO122 |
| A | GLU123 |
| A | GOL1721 |
| A | HOH2148 |
| A | GLY60 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3001 |
| Chain | Residue |
| B | PRO191 |
| B | ILE192 |
| B | GLU193 |
| B | ARG196 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1719 |
| Chain | Residue |
| B | GLY60 |
| B | ALA61 |
| B | PHE66 |
| B | GLY99 |
| B | GLY100 |
| B | GLU123 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1720 |
| Chain | Residue |
| A | TRP594 |
| B | GLY305 |
| B | THR306 |
| B | ARG309 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1723 |
| Chain | Residue |
| A | ASN207 |
| A | ASP209 |
| A | SER210 |
| A | GLY553 |
| A | ASN554 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3001 |
| Chain | Residue |
| A | PRO191 |
| A | ILE192 |
| A | GLU193 |
| A | ARG196 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3001 |
| 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 | 560 |
| Details | Region: {"description":"Enoyl-CoA hydratase / isomerase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 578 |
| Details | Region: {"description":"3-hydroxyacyl-CoA dehydrogenase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Blocked amino end (Ala)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 18 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBM2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 14 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DBM2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBM2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q08426","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q08426","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
