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 |