5KAG
Crystal structure of a dioxygenase in the Crotonase superfamily in P21
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006635 | biological_process | fatty acid beta-oxidation |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0006635 | biological_process | fatty acid beta-oxidation |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| E | 0017000 | biological_process | antibiotic biosynthetic process |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0006635 | biological_process | fatty acid beta-oxidation |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| F | 0017000 | biological_process | antibiotic biosynthetic process |
| F | 0042802 | molecular_function | identical protein binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0006635 | biological_process | fatty acid beta-oxidation |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| G | 0017000 | biological_process | antibiotic biosynthetic process |
| G | 0042802 | molecular_function | identical protein binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0006635 | biological_process | fatty acid beta-oxidation |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| H | 0017000 | biological_process | antibiotic biosynthetic process |
| H | 0042802 | molecular_function | identical protein binding |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0006635 | biological_process | fatty acid beta-oxidation |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| I | 0017000 | biological_process | antibiotic biosynthetic process |
| I | 0042802 | molecular_function | identical protein binding |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0006635 | biological_process | fatty acid beta-oxidation |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| J | 0017000 | biological_process | antibiotic biosynthetic process |
| J | 0042802 | molecular_function | identical protein binding |
| K | 0003824 | molecular_function | catalytic activity |
| K | 0006635 | biological_process | fatty acid beta-oxidation |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| K | 0017000 | biological_process | antibiotic biosynthetic process |
| K | 0042802 | molecular_function | identical protein binding |
| L | 0003824 | molecular_function | catalytic activity |
| L | 0006635 | biological_process | fatty acid beta-oxidation |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| L | 0017000 | biological_process | antibiotic biosynthetic process |
| L | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue YE1 A 501 |
| Chain | Residue |
| A | ASP184 |
| A | ILE235 |
| A | ASN236 |
| A | LEU237 |
| A | LYS238 |
| A | PHE250 |
| A | ARG254 |
| A | PHE292 |
| A | ILE294 |
| A | GLY295 |
| A | GLY296 |
| A | ARG185 |
| A | GLN299 |
| A | TYR314 |
| A | ILE324 |
| A | ILE325 |
| A | GLY327 |
| A | GLN416 |
| A | PHE432 |
| A | OXY502 |
| A | HOH627 |
| A | HOH653 |
| A | ALA188 |
| A | GLU189 |
| A | HIS222 |
| A | ARG224 |
| A | TYR225 |
| A | ALA233 |
| A | GLY234 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue OXY A 502 |
| Chain | Residue |
| A | LEU237 |
| A | YE1501 |
| A | HOH655 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue YE1 B 501 |
| Chain | Residue |
| B | ALA188 |
| B | GLU189 |
| B | HIS222 |
| B | ARG224 |
| B | TYR225 |
| B | ALA233 |
| B | GLY234 |
| B | ILE235 |
| B | ASN236 |
| B | LEU237 |
| B | LYS238 |
| B | PHE250 |
| B | ARG254 |
| B | ILE294 |
| B | GLY295 |
| B | GLY296 |
| B | GLN299 |
| B | ILE324 |
| B | ILE325 |
| B | GLY327 |
| B | GLN416 |
| B | PHE432 |
| B | OXY502 |
| B | HOH648 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue OXY B 502 |
| Chain | Residue |
| B | ALA319 |
| B | GLY323 |
| B | ILE324 |
| B | YE1501 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | binding site for residue YE1 C 501 |
| Chain | Residue |
| C | ARG185 |
| C | LEU186 |
| C | ALA188 |
| C | GLU189 |
| C | HIS222 |
| C | TYR225 |
| C | ALA233 |
| C | GLY234 |
| C | ILE235 |
| C | ASN236 |
| C | LEU237 |
| C | LYS238 |
| C | PHE250 |
| C | LEU251 |
| C | ARG254 |
| C | PHE292 |
| C | ILE294 |
| C | GLY295 |
| C | GLY296 |
| C | GLN299 |
| C | ILE324 |
| C | ILE325 |
| C | GLY327 |
| C | GLN416 |
| C | PHE432 |
| C | OXY502 |
| C | HOH603 |
| C | HOH622 |
| C | HOH627 |
| C | HOH643 |
| C | HOH656 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue OXY C 502 |
| Chain | Residue |
| C | LEU237 |
| C | ALA319 |
| C | YE1501 |
| C | HOH627 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue YE1 D 501 |
| Chain | Residue |
| D | ARG224 |
| D | TYR225 |
| D | ALA233 |
| D | GLY234 |
| D | ILE235 |
| D | ASN236 |
| D | LEU237 |
| D | LYS238 |
| D | PHE250 |
| D | LEU251 |
| D | ARG254 |
| D | ILE294 |
| D | GLY295 |
| D | GLY296 |
| D | GLN299 |
| D | ILE324 |
| D | ILE325 |
| D | GLY327 |
| D | GLN416 |
| D | PHE432 |
| D | OXY502 |
| D | HOH605 |
| D | HOH652 |
| D | LEU186 |
| D | ALA188 |
| D | GLU189 |
| D | HIS222 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OXY D 502 |
| Chain | Residue |
| D | ALA319 |
| D | GLY323 |
| D | ILE324 |
| D | YE1501 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | binding site for residue YE1 E 501 |
| Chain | Residue |
| E | ARG185 |
| E | LEU186 |
| E | ALA188 |
| E | GLU189 |
| E | HIS222 |
| E | ARG224 |
| E | TYR225 |
| E | ALA233 |
| E | GLY234 |
| E | ILE235 |
| E | ASN236 |
| E | LEU237 |
| E | LYS238 |
| E | PHE250 |
| E | LEU251 |
| E | ARG254 |
| E | ILE294 |
| E | GLY295 |
| E | GLY296 |
| E | GLN299 |
| E | ILE324 |
| E | ILE325 |
| E | GLY327 |
| E | GLN416 |
| E | PHE432 |
| E | OXY502 |
| E | HOH605 |
| E | HOH620 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue OXY E 502 |
| Chain | Residue |
| E | ALA319 |
| E | GLY323 |
| E | ILE324 |
| E | LYS428 |
| E | YE1501 |
| site_id | AD2 |
| Number of Residues | 29 |
| Details | binding site for residue YE1 F 501 |
| Chain | Residue |
| F | LEU186 |
| F | ALA188 |
| F | GLU189 |
| F | HIS222 |
| F | ARG224 |
| F | TYR225 |
| F | ALA233 |
| F | GLY234 |
| F | ILE235 |
| F | ASN236 |
| F | LEU237 |
| F | LYS238 |
| F | PHE250 |
| F | LEU251 |
| F | ARG254 |
| F | PHE292 |
| F | GLY295 |
| F | GLY296 |
| F | GLN299 |
| F | TYR314 |
| F | PRO318 |
| F | ILE324 |
| F | ILE325 |
| F | GLY327 |
| F | GLN416 |
| F | PHE432 |
| F | OXY502 |
| F | HOH627 |
| F | HOH651 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue OXY F 502 |
| Chain | Residue |
| F | ALA319 |
| F | YE1501 |
| site_id | AD4 |
| Number of Residues | 26 |
| Details | binding site for residue YE1 G 501 |
| Chain | Residue |
| G | ARG185 |
| G | LEU186 |
| G | ALA188 |
| G | GLU189 |
| G | HIS222 |
| G | ARG224 |
| G | TYR225 |
| G | ALA233 |
| G | GLY234 |
| G | ILE235 |
| G | ASN236 |
| G | LEU237 |
| G | LYS238 |
| G | PHE250 |
| G | ARG254 |
| G | ILE294 |
| G | GLY295 |
| G | GLY296 |
| G | GLN299 |
| G | ILE324 |
| G | ILE325 |
| G | GLY327 |
| G | GLN416 |
| G | PHE432 |
| G | OXY502 |
| G | HOH617 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue OXY G 502 |
| Chain | Residue |
| G | ALA319 |
| G | GLY323 |
| G | ILE324 |
| G | YE1501 |
| site_id | AD6 |
| Number of Residues | 28 |
| Details | binding site for residue YE1 H 501 |
| Chain | Residue |
| H | ARG185 |
| H | LEU186 |
| H | ALA188 |
| H | GLU189 |
| H | HIS222 |
| H | ARG224 |
| H | TYR225 |
| H | ALA233 |
| H | GLY234 |
| H | ILE235 |
| H | ASN236 |
| H | LEU237 |
| H | LYS238 |
| H | PHE250 |
| H | LEU251 |
| H | ARG254 |
| H | ILE294 |
| H | GLY295 |
| H | GLY296 |
| H | GLN299 |
| H | PRO318 |
| H | ILE324 |
| H | ILE325 |
| H | GLY327 |
| H | GLN416 |
| H | PHE432 |
| H | OXY502 |
| H | HOH634 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue OXY H 502 |
| Chain | Residue |
| H | ALA319 |
| H | GLY323 |
| H | ILE324 |
| H | YE1501 |
| site_id | AD8 |
| Number of Residues | 27 |
| Details | binding site for residue YE1 I 501 |
| Chain | Residue |
| I | ALA188 |
| I | GLU189 |
| I | HIS222 |
| I | ARG224 |
| I | TYR225 |
| I | ALA233 |
| I | GLY234 |
| I | ILE235 |
| I | ASN236 |
| I | LEU237 |
| I | LYS238 |
| I | PHE250 |
| I | LEU251 |
| I | ARG254 |
| I | ILE294 |
| I | GLY295 |
| I | GLY296 |
| I | GLN299 |
| I | ILE324 |
| I | ILE325 |
| I | GLY327 |
| I | GLN416 |
| I | PHE432 |
| I | OXY502 |
| I | HOH617 |
| I | HOH619 |
| I | HOH654 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue OXY I 502 |
| Chain | Residue |
| I | ALA319 |
| I | GLY323 |
| I | ILE324 |
| I | YE1501 |
| I | HOH619 |
| site_id | AE1 |
| Number of Residues | 30 |
| Details | binding site for residue YE1 J 501 |
| Chain | Residue |
| J | ARG185 |
| J | LEU186 |
| J | ALA188 |
| J | GLU189 |
| J | HIS222 |
| J | ARG224 |
| J | TYR225 |
| J | ALA233 |
| J | GLY234 |
| J | ILE235 |
| J | ASN236 |
| J | LEU237 |
| J | LYS238 |
| J | PHE250 |
| J | LEU251 |
| J | ARG254 |
| J | PHE292 |
| J | ILE294 |
| J | GLY295 |
| J | GLY296 |
| J | GLN299 |
| J | PRO318 |
| J | ILE324 |
| J | ILE325 |
| J | GLY327 |
| J | PHE412 |
| J | GLN416 |
| J | PHE432 |
| J | OXY502 |
| J | HOH619 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue OXY J 502 |
| Chain | Residue |
| J | LEU237 |
| J | YE1501 |
| site_id | AE3 |
| Number of Residues | 30 |
| Details | binding site for residue YE1 K 501 |
| Chain | Residue |
| K | ARG185 |
| K | LEU186 |
| K | ALA188 |
| K | GLU189 |
| K | HIS222 |
| K | ARG224 |
| K | TYR225 |
| K | ALA233 |
| K | GLY234 |
| K | ILE235 |
| K | ASN236 |
| K | LEU237 |
| K | LYS238 |
| K | PHE250 |
| K | LEU251 |
| K | ARG254 |
| K | PHE292 |
| K | ILE294 |
| K | GLY295 |
| K | GLY296 |
| K | GLN299 |
| K | ILE324 |
| K | ILE325 |
| K | GLY327 |
| K | GLN416 |
| K | PHE432 |
| K | OXY502 |
| K | HOH614 |
| K | HOH634 |
| K | HOH668 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue OXY K 502 |
| Chain | Residue |
| K | ALA319 |
| K | GLY323 |
| K | ILE324 |
| K | YE1501 |
| K | HOH614 |
| site_id | AE5 |
| Number of Residues | 26 |
| Details | binding site for residue YE1 L 501 |
| Chain | Residue |
| L | ARG185 |
| L | LEU186 |
| L | ALA188 |
| L | GLU189 |
| L | HIS222 |
| L | ARG224 |
| L | TYR225 |
| L | ALA233 |
| L | GLY234 |
| L | ILE235 |
| L | ASN236 |
| L | LEU237 |
| L | LYS238 |
| L | PHE250 |
| L | ARG254 |
| L | ILE294 |
| L | GLY295 |
| L | GLY296 |
| L | GLN299 |
| L | ILE324 |
| L | ILE325 |
| L | GLY327 |
| L | GLN416 |
| L | PHE432 |
| L | OXY502 |
| L | HOH603 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue OXY L 502 |
| Chain | Residue |
| L | ALA319 |
| L | YE1501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 168 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18004875","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
