5U8Z
Structure of Fe-CAO1 in complex with beta-fluororesveratrol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010436 | molecular_function | carotenoid dioxygenase activity |
| A | 0016121 | biological_process | carotene catabolic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0010436 | molecular_function | carotenoid dioxygenase activity |
| B | 0016121 | biological_process | carotene catabolic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0010436 | molecular_function | carotenoid dioxygenase activity |
| C | 0016121 | biological_process | carotene catabolic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0010436 | molecular_function | carotenoid dioxygenase activity |
| D | 0016121 | biological_process | carotene catabolic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 A 601 |
| Chain | Residue |
| A | HIS197 |
| A | HIS248 |
| A | HIS313 |
| A | HIS510 |
| A | HOH873 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue 83D A 602 |
| Chain | Residue |
| A | GLU165 |
| A | HIS248 |
| A | GLY312 |
| A | HIS313 |
| A | PHE337 |
| A | GLU383 |
| A | PHE384 |
| A | LEU509 |
| A | HOH857 |
| A | HOH873 |
| A | HOH985 |
| A | PHE91 |
| A | TYR133 |
| A | THR151 |
| A | LYS164 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 603 |
| Chain | Residue |
| A | ARG112 |
| A | THR179 |
| A | HOH983 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 604 |
| Chain | Residue |
| A | PHE384 |
| A | PRO425 |
| A | THR451 |
| A | GLY508 |
| A | HOH967 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 601 |
| Chain | Residue |
| B | HIS197 |
| B | HIS248 |
| B | HIS313 |
| B | HIS510 |
| B | 83D602 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue 83D B 602 |
| Chain | Residue |
| B | PHE91 |
| B | TYR133 |
| B | THR151 |
| B | LYS164 |
| B | GLU165 |
| B | HIS248 |
| B | GLY312 |
| B | HIS313 |
| B | PHE337 |
| B | GLU383 |
| B | PHE384 |
| B | LEU509 |
| B | FE2601 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 603 |
| Chain | Residue |
| B | ARG112 |
| B | THR179 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 C 601 |
| Chain | Residue |
| C | HIS197 |
| C | HIS248 |
| C | HIS313 |
| C | HIS510 |
| C | 83D602 |
| C | HOH802 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue 83D C 602 |
| Chain | Residue |
| C | PHE91 |
| C | TYR133 |
| C | THR151 |
| C | LYS164 |
| C | GLU165 |
| C | HIS248 |
| C | GLY312 |
| C | HIS313 |
| C | PHE337 |
| C | GLU383 |
| C | PHE384 |
| C | LEU509 |
| C | FE2601 |
| C | HOH802 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 603 |
| Chain | Residue |
| C | ARG112 |
| C | THR179 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 D 601 |
| Chain | Residue |
| D | HIS197 |
| D | HIS248 |
| D | HIS313 |
| D | HIS510 |
| D | 83D602 |
| D | HOH721 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue 83D D 602 |
| Chain | Residue |
| D | PHE91 |
| D | TYR133 |
| D | THR151 |
| D | LYS164 |
| D | GLU165 |
| D | HIS248 |
| D | GLY312 |
| D | HIS313 |
| D | PHE337 |
| D | GLU383 |
| D | LEU509 |
| D | FE2601 |
| D | HOH721 |
| D | HOH898 |
| D | HOH1046 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 603 |
| Chain | Residue |
| D | ARG112 |
| D | THR179 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 604 |
| Chain | Residue |
| D | PHE384 |
| D | PRO425 |
| D | GLY452 |
| D | GLY508 |
| D | HOH1009 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28493664","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5U90","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28493664","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5U8X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
