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 | 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 | 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 | 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 | 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: BINDING => ECO:0000269|PubMed:28493664, ECO:0007744|PDB:5U90 |
Chain | Residue | Details |
A | TYR133 | |
D | TYR133 | |
D | LYS164 | |
D | GLU383 | |
A | LYS164 | |
A | GLU383 | |
B | TYR133 | |
B | LYS164 | |
B | GLU383 | |
C | TYR133 | |
C | LYS164 | |
C | GLU383 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28493664, ECO:0007744|PDB:5U8X |
Chain | Residue | Details |
A | HIS197 | |
C | HIS248 | |
C | HIS313 | |
C | HIS510 | |
D | HIS197 | |
D | HIS248 | |
D | HIS313 | |
D | HIS510 | |
A | HIS248 | |
A | HIS313 | |
A | HIS510 | |
B | HIS197 | |
B | HIS248 | |
B | HIS313 | |
B | HIS510 | |
C | HIS197 |