2NP9
Crystal structure of a dioxygenase in the Crotonase superfamily
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE YE1 A 999 |
| Chain | Residue |
| A | LEU186 |
| A | LEU237 |
| A | LYS238 |
| A | LEU251 |
| A | ARG254 |
| A | PHE292 |
| A | GLY295 |
| A | GLY296 |
| A | GLN299 |
| A | PRO318 |
| A | GLY327 |
| A | ALA188 |
| A | PHE432 |
| A | HOH1068 |
| A | GLU189 |
| A | HIS222 |
| A | TYR225 |
| A | ALA233 |
| A | GLY234 |
| A | ILE235 |
| A | ASN236 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE YE1 B 999 |
| 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 | PHE292 |
| B | GLY295 |
| B | GLY296 |
| B | ILE324 |
| B | ILE325 |
| B | GLY327 |
| B | GLN416 |
| B | PHE432 |
| B | OXY888 |
| B | HOH1032 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE YE1 C 999 |
| Chain | Residue |
| 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 | GLY295 |
| C | GLY296 |
| C | GLN299 |
| C | PRO318 |
| C | ILE324 |
| C | ILE325 |
| C | GLY327 |
| C | PHE432 |
| C | OXY888 |
| C | HOH1052 |
| C | HOH1057 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OXY A 888 |
| Chain | Residue |
| A | ALA319 |
| A | GLY323 |
| A | ILE324 |
| A | HOH1070 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OXY B 888 |
| Chain | Residue |
| B | ALA319 |
| B | GLY323 |
| B | ILE324 |
| B | YE1999 |
| B | HOH1055 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OXY C 888 |
| Chain | Residue |
| C | ALA319 |
| C | GLY323 |
| C | ILE324 |
| C | YE1999 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18004875 |
| Chain | Residue | Details |
| A | ASP183 | |
| B | HIS222 | |
| B | ALA233 | |
| B | GLY296 | |
| B | ILE325 | |
| B | GLN416 | |
| C | ASP183 | |
| C | GLU189 | |
| C | HIS222 | |
| C | ALA233 | |
| C | GLY296 | |
| A | GLU189 | |
| C | ILE325 | |
| C | GLN416 | |
| A | HIS222 | |
| A | ALA233 | |
| A | GLY296 | |
| A | ILE325 | |
| A | GLN416 | |
| B | ASP183 | |
| B | GLU189 |
