4FC6
Studies on DCR shed new light on peroxisomal beta-oxidation: Crystal structure of the ternary complex of pDCR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005778 | cellular_component | peroxisomal membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| A | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| A | 0009062 | biological_process | fatty acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0051020 | molecular_function | GTPase binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005778 | cellular_component | peroxisomal membrane |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| B | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| B | 0009062 | biological_process | fatty acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| B | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0051020 | molecular_function | GTPase binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005778 | cellular_component | peroxisomal membrane |
| C | 0005829 | cellular_component | cytosol |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| C | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| C | 0009062 | biological_process | fatty acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| C | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| C | 0044877 | molecular_function | protein-containing complex binding |
| C | 0051020 | molecular_function | GTPase binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005778 | cellular_component | peroxisomal membrane |
| D | 0005829 | cellular_component | cytosol |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| D | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| D | 0009062 | biological_process | fatty acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| D | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| D | 0044877 | molecular_function | protein-containing complex binding |
| D | 0051020 | molecular_function | GTPase binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 401 |
| Chain | Residue |
| A | GLY35 |
| A | ASP86 |
| A | VAL87 |
| A | ARG88 |
| A | CYS113 |
| A | ALA114 |
| A | ALA115 |
| A | ILE163 |
| A | THR164 |
| A | LYS182 |
| A | PRO208 |
| A | SER38 |
| A | GLY209 |
| A | PRO210 |
| A | ILE211 |
| A | THR214 |
| A | GLU215 |
| A | GLY216 |
| A | LEU217 |
| A | HXC402 |
| A | HOH502 |
| A | HOH506 |
| A | GLY39 |
| A | HOH535 |
| A | HOH536 |
| A | HOH570 |
| C | HOH497 |
| A | ILE40 |
| A | SER59 |
| A | ARG60 |
| A | SER61 |
| A | ARG64 |
| A | MET85 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HXC A 402 |
| Chain | Residue |
| A | ARG60 |
| A | ARG88 |
| A | ALA115 |
| A | GLY116 |
| A | ASN117 |
| A | PHE118 |
| A | CYS120 |
| A | SER126 |
| A | ASN128 |
| A | ALA129 |
| A | THR132 |
| A | ILE136 |
| A | GLY216 |
| A | ARG219 |
| A | LEU220 |
| A | NAP401 |
| A | HOH518 |
| A | HOH534 |
| A | HOH550 |
| A | HOH589 |
| A | HOH594 |
| A | HOH622 |
| A | HOH623 |
| A | HOH633 |
| A | HOH644 |
| A | HOH671 |
| A | HOH680 |
| C | ARG27 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP B 401 |
| Chain | Residue |
| B | GLY35 |
| B | SER38 |
| B | GLY39 |
| B | ILE40 |
| B | SER59 |
| B | ARG60 |
| B | SER61 |
| B | ARG64 |
| B | MET85 |
| B | ASP86 |
| B | VAL87 |
| B | ARG88 |
| B | CYS113 |
| B | ALA114 |
| B | ALA115 |
| B | ILE136 |
| B | ILE163 |
| B | THR164 |
| B | LYS182 |
| B | PRO208 |
| B | GLY209 |
| B | PRO210 |
| B | ILE211 |
| B | THR214 |
| B | GLU215 |
| B | GLY216 |
| B | HXC402 |
| B | HOH504 |
| B | HOH508 |
| B | HOH528 |
| B | HOH550 |
| B | HOH615 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE HXC B 402 |
| Chain | Residue |
| B | PHE118 |
| B | CYS120 |
| B | SER126 |
| B | ASN128 |
| B | ALA129 |
| B | THR132 |
| B | ILE136 |
| B | LEU167 |
| B | GLU215 |
| B | ARG219 |
| B | LEU220 |
| B | NAP401 |
| B | HOH520 |
| B | HOH532 |
| B | HOH545 |
| B | HOH559 |
| B | HOH562 |
| B | HOH565 |
| B | HOH590 |
| B | HOH623 |
| B | HOH625 |
| B | HOH630 |
| B | HOH665 |
| B | TYR17 |
| B | ARG18 |
| B | ARG60 |
| B | ARG88 |
| B | GLY116 |
| B | ASN117 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HXC C 301 |
| Chain | Residue |
| C | ARG60 |
| C | ARG88 |
| C | ALA115 |
| C | GLY116 |
| C | ASN117 |
| C | PHE118 |
| C | SER126 |
| C | ASN128 |
| C | ALA129 |
| C | THR132 |
| C | ILE136 |
| C | GLY216 |
| C | ARG219 |
| C | LEU220 |
| C | NAP302 |
| C | HOH415 |
| C | HOH418 |
| C | HOH422 |
| C | HOH430 |
| C | HOH451 |
| C | HOH458 |
| C | HOH477 |
| C | HOH479 |
| C | HOH505 |
| C | HOH574 |
| C | HOH583 |
| site_id | AC6 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP C 302 |
| Chain | Residue |
| C | GLY35 |
| C | SER38 |
| C | GLY39 |
| C | ILE40 |
| C | SER59 |
| C | ARG60 |
| C | SER61 |
| C | ARG64 |
| C | MET85 |
| C | ASP86 |
| C | VAL87 |
| C | ARG88 |
| C | CYS113 |
| C | ALA114 |
| C | ALA115 |
| C | ILE136 |
| C | ILE163 |
| C | THR164 |
| C | LYS182 |
| C | PRO208 |
| C | GLY209 |
| C | PRO210 |
| C | ILE211 |
| C | THR214 |
| C | GLU215 |
| C | GLY216 |
| C | HXC301 |
| C | HOH408 |
| C | HOH432 |
| C | HOH434 |
| C | HOH451 |
| C | HOH457 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP D 401 |
| Chain | Residue |
| D | GLY35 |
| D | SER38 |
| D | GLY39 |
| D | ILE40 |
| D | SER59 |
| D | ARG60 |
| D | SER61 |
| D | ARG64 |
| D | MET85 |
| D | ASP86 |
| D | VAL87 |
| D | ARG88 |
| D | CYS113 |
| D | ALA114 |
| D | ALA115 |
| D | ILE163 |
| D | THR164 |
| D | LYS182 |
| D | PRO208 |
| D | GLY209 |
| D | PRO210 |
| D | ILE211 |
| D | THR214 |
| D | GLU215 |
| D | GLY216 |
| D | HXC402 |
| D | HOH506 |
| D | HOH508 |
| D | HOH531 |
| D | HOH550 |
| D | HOH552 |
| D | HOH581 |
| D | HOH628 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HXC D 402 |
| Chain | Residue |
| D | ARG60 |
| D | ARG88 |
| D | ALA115 |
| D | GLY116 |
| D | ASN117 |
| D | PHE118 |
| D | CYS120 |
| D | SER126 |
| D | ASN128 |
| D | ALA129 |
| D | THR132 |
| D | GLU215 |
| D | GLY216 |
| D | ARG219 |
| D | LEU220 |
| D | NAP401 |
| D | HOH511 |
| D | HOH519 |
| D | HOH536 |
| D | HOH543 |
| D | HOH553 |
| D | HOH577 |
| D | HOH599 |
| D | HOH625 |
| D | HOH649 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 68 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22745130","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
