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