5U90
Crystal structure of Co-CAO1 in complex with resveratrol
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 CO A 601 |
| Chain | Residue |
| A | HIS197 |
| A | HIS248 |
| A | HIS313 |
| A | HIS510 |
| A | HOH797 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue STL A 602 |
| Chain | Residue |
| A | GLU165 |
| A | HIS248 |
| A | GLY312 |
| A | HIS313 |
| A | PHE337 |
| A | GLU383 |
| A | PHE384 |
| A | PRO425 |
| A | STL605 |
| A | HOH706 |
| A | HOH876 |
| A | PHE91 |
| A | TYR133 |
| A | THR151 |
| A | LYS164 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 603 |
| Chain | Residue |
| A | GLU478 |
| A | ASP479 |
| A | MET480 |
| A | HOH715 |
| D | GLU478 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 604 |
| Chain | Residue |
| A | TYR137 |
| A | THR138 |
| A | LYS272 |
| A | GLN273 |
| A | GLY274 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue STL A 605 |
| Chain | Residue |
| A | ASN41 |
| A | PHE338 |
| A | TRP339 |
| A | GLY423 |
| A | PRO425 |
| A | STL602 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue STL A 606 |
| Chain | Residue |
| A | LYS144 |
| A | HOH711 |
| C | TYR282 |
| C | ASP342 |
| C | ASN344 |
| C | LYS346 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue STL A 607 |
| Chain | Residue |
| A | GLU414 |
| A | MET417 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue CO B 601 |
| Chain | Residue |
| B | HIS197 |
| B | HIS248 |
| B | HIS313 |
| B | HIS510 |
| B | HOH734 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue STL 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 | PRO425 |
| B | HOH840 |
| B | HOH949 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 603 |
| Chain | Residue |
| B | TYR155 |
| B | ASP515 |
| B | ASP518 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 604 |
| Chain | Residue |
| B | LYS215 |
| B | TRP238 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 605 |
| Chain | Residue |
| B | LEU444 |
| B | THR493 |
| B | GLU495 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 606 |
| Chain | Residue |
| D | ASP412 |
| D | ARG448 |
| D | STL607 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 607 |
| Chain | Residue |
| B | GLU478 |
| B | ASP479 |
| B | MET480 |
| B | HOH749 |
| C | ASP479 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue CO C 601 |
| Chain | Residue |
| C | HIS197 |
| C | HIS248 |
| C | HIS313 |
| C | HIS510 |
| C | HOH786 |
| site_id | AD7 |
| Number of Residues | 14 |
| Details | binding site for residue STL 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 | PRO425 |
| C | HOH770 |
| C | HOH886 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue STL C 603 |
| Chain | Residue |
| A | GLY187 |
| A | LEU189 |
| A | PRO190 |
| A | LEU192 |
| A | LYS215 |
| C | SER283 |
| C | HOH1016 |
| A | ASP184 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue CO D 601 |
| Chain | Residue |
| D | HIS197 |
| D | HIS248 |
| D | HIS313 |
| D | HIS510 |
| D | HOH761 |
| site_id | AE1 |
| Number of Residues | 15 |
| Details | binding site for residue STL 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 | PHE384 |
| D | PRO425 |
| D | STL606 |
| D | HOH811 |
| D | HOH963 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 603 |
| Chain | Residue |
| D | ASP515 |
| D | ASP518 |
| D | VAL519 |
| D | HOH861 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 604 |
| Chain | Residue |
| B | ARG220 |
| B | VAL240 |
| D | CYS266 |
| D | HOH867 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue DMS D 605 |
| Chain | Residue |
| D | HIS356 |
| D | TYR376 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue STL D 606 |
| Chain | Residue |
| D | PHE338 |
| D | TRP339 |
| D | GLY423 |
| D | ALA424 |
| D | PRO425 |
| D | STL602 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue STL D 607 |
| Chain | Residue |
| B | GLU305 |
| B | LEU371 |
| B | DMS606 |
| D | PRO408 |
| D | GLY409 |
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 |
