6VSH
Crystal structure of apo Dicamba Monooxygenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0009056 | biological_process | catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0009056 | biological_process | catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0009056 | biological_process | catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue FES A 501 |
| Chain | Residue |
| A | CYS49 |
| A | HIS51 |
| A | ARG52 |
| A | CYS68 |
| A | HIS71 |
| A | LEU73 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue FES B 501 |
| Chain | Residue |
| B | CYS68 |
| B | HIS71 |
| B | LEU73 |
| B | CYS49 |
| B | HIS51 |
| B | ARG52 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue FES C 501 |
| Chain | Residue |
| C | CYS49 |
| C | HIS51 |
| C | CYS68 |
| C | HIS71 |
| C | LEU73 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19616009, ECO:0000269|PubMed:19616011, ECO:0007744|PDB:3GB4, ECO:0007744|PDB:3GKE, ECO:0007744|PDB:3GL0, ECO:0007744|PDB:3GL2, ECO:0007744|PDB:3GOB, ECO:0007744|PDB:3GTE, ECO:0007744|PDB:3GTS |
| Chain | Residue | Details |
| A | CYS49 | |
| B | CYS68 | |
| B | HIS71 | |
| B | HIS160 | |
| B | HIS165 | |
| B | ASP294 | |
| C | CYS49 | |
| C | HIS51 | |
| C | CYS68 | |
| C | HIS71 | |
| C | HIS160 | |
| A | HIS51 | |
| C | HIS165 | |
| C | ASP294 | |
| A | CYS68 | |
| A | HIS71 | |
| A | HIS160 | |
| A | HIS165 | |
| A | ASP294 | |
| B | CYS49 | |
| B | HIS51 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19616009, ECO:0000269|PubMed:19616011, ECO:0007744|PDB:3GB4, ECO:0007744|PDB:3GKE, ECO:0007744|PDB:3GL0, ECO:0007744|PDB:3GL2, ECO:0007744|PDB:3GOB, ECO:0007744|PDB:3GTS |
| Chain | Residue | Details |
| A | ASN230 | |
| A | HIS251 | |
| B | ASN230 | |
| B | HIS251 | |
| C | ASN230 | |
| C | HIS251 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19616009, ECO:0000269|PubMed:19616011, ECO:0007744|PDB:3GB4, ECO:0007744|PDB:3GKE, ECO:0007744|PDB:3GL0, ECO:0007744|PDB:3GL2, ECO:0007744|PDB:3GTS |
| Chain | Residue | Details |
| A | TRP285 | |
| B | TRP285 | |
| C | TRP285 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | SITE: Plays a role in the stabilization of the metal coordination => ECO:0000269|PubMed:19616009 |
| Chain | Residue | Details |
| A | ASN154 | |
| B | ASN154 | |
| C | ASN154 |
