3ZWB
CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 1 (RPMFE1) COMPLEXED WITH 2TRANS-HEXENOYL-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 | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1721 |
Chain | Residue |
A | MET307 |
A | VAL381 |
A | ASN408 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1722 |
Chain | Residue |
A | ARG30 |
A | LYS680 |
A | ARG683 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE TC6 A 1723 |
Chain | Residue |
A | ALA59 |
A | GLY60 |
A | ALA61 |
A | ASP62 |
A | ILE63 |
A | LEU98 |
A | GLY100 |
A | GLU103 |
A | GLY131 |
A | TYR156 |
A | LYS275 |
A | HOH2006 |
A | HOH2009 |
B | LYS249 |
A | PRO20 |
A | VAL21 |
A | ALA23 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1724 |
Chain | Residue |
A | PRO191 |
A | ILE192 |
A | GLU193 |
A | ARG196 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1719 |
Chain | Residue |
B | SER521 |
B | ARG533 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1720 |
Chain | Residue |
B | LEU73 |
B | ALA74 |
B | LEU75 |
B | GLY76 |
B | SER77 |
B | ARG133 |
site_id | AC7 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE TC6 B 1721 |
Chain | Residue |
B | PRO20 |
B | VAL21 |
B | ALA59 |
B | GLY60 |
B | ALA61 |
B | ASP62 |
B | ILE63 |
B | PHE66 |
B | LEU98 |
B | GLY100 |
B | GLU103 |
B | PRO122 |
B | GLY131 |
B | ALA132 |
B | TYR156 |
B | PHE255 |
B | LYS275 |
B | LYS279 |
B | LYS463 |
B | HOH2013 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1722 |
Chain | Residue |
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 | ALA123 | |
B | GLU103 | |
B | ALA123 |
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 |