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 | 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 |
B | 0005515 | molecular_function | protein binding |
B | 0005777 | cellular_component | peroxisome |
B | 0005778 | cellular_component | peroxisomal membrane |
B | 0005829 | cellular_component | cytosol |
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 |
C | 0005515 | molecular_function | protein binding |
C | 0005777 | cellular_component | peroxisome |
C | 0005778 | cellular_component | peroxisomal membrane |
C | 0005829 | cellular_component | cytosol |
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 |
D | 0005515 | molecular_function | protein binding |
D | 0005777 | cellular_component | peroxisome |
D | 0005778 | cellular_component | peroxisomal membrane |
D | 0005829 | cellular_component | cytosol |
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 |
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 | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22745130 |
Chain | Residue | Details |
A | GLY35 | |
C | ASP86 | |
C | LYS182 | |
C | PRO208 | |
D | GLY35 | |
D | ASP86 | |
D | LYS182 | |
D | PRO208 | |
A | ASP86 | |
A | LYS182 | |
A | PRO208 | |
B | GLY35 | |
B | ASP86 | |
B | LYS182 | |
B | PRO208 | |
C | GLY35 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG60 | |
B | ARG219 | |
C | ARG60 | |
C | ARG88 | |
C | PHE118 | |
C | SER126 | |
C | ARG219 | |
D | ARG60 | |
D | ARG88 | |
D | PHE118 | |
D | SER126 | |
A | ARG88 | |
D | ARG219 | |
A | PHE118 | |
A | SER126 | |
A | ARG219 | |
B | ARG60 | |
B | ARG88 | |
B | PHE118 | |
B | SER126 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 | |
C | ALA2 | |
D | ALA2 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS151 | |
B | LYS151 | |
C | LYS151 | |
D | LYS151 |