1FOH
PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM
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 | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0018662 | molecular_function | phenol 2-monooxygenase activity |
| A | 0019336 | biological_process | phenol-containing compound catabolic process |
| A | 0071949 | molecular_function | FAD binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0009056 | biological_process | catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| B | 0018662 | molecular_function | phenol 2-monooxygenase activity |
| B | 0019336 | biological_process | phenol-containing compound catabolic process |
| B | 0071949 | molecular_function | FAD binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0009056 | biological_process | catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| C | 0018662 | molecular_function | phenol 2-monooxygenase activity |
| C | 0019336 | biological_process | phenol-containing compound catabolic process |
| C | 0071949 | molecular_function | FAD binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0009056 | biological_process | catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| D | 0018662 | molecular_function | phenol 2-monooxygenase activity |
| D | 0019336 | biological_process | phenol-containing compound catabolic process |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 801 |
| Chain | Residue |
| A | VAL13 |
| A | GLN117 |
| A | PRO144 |
| A | CYS224 |
| A | ASP225 |
| A | GLY226 |
| A | ARG287 |
| A | TYR289 |
| A | TRP332 |
| A | GLY356 |
| A | ASP357 |
| A | GLY14 |
| A | PRO364 |
| A | GLY369 |
| A | MET370 |
| A | SER373 |
| A | HOH806 |
| A | HOH894 |
| A | HOH896 |
| A | HOH951 |
| A | HOH970 |
| A | HOH998 |
| A | GLY16 |
| A | PRO17 |
| A | ALA18 |
| A | ASP42 |
| A | LYS43 |
| A | ARG44 |
| A | ALA53 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPH A 802 |
| Chain | Residue |
| A | ASP54 |
| A | GLN112 |
| A | ARG265 |
| A | ILE279 |
| A | TYR289 |
| A | PRO364 |
| A | ALA366 |
| A | GLY367 |
| A | HOH1092 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 801 |
| Chain | Residue |
| B | GLY14 |
| B | GLY16 |
| B | PRO17 |
| B | ALA18 |
| B | ASP42 |
| B | LYS43 |
| B | ARG44 |
| B | ALA53 |
| B | GLN117 |
| B | PRO144 |
| B | CYS224 |
| B | ASP225 |
| B | GLY226 |
| B | VAL250 |
| B | ARG287 |
| B | TYR289 |
| B | GLY356 |
| B | ASP357 |
| B | PRO364 |
| B | GLY369 |
| B | MET370 |
| B | SER373 |
| B | HOH806 |
| B | HOH897 |
| B | HOH918 |
| B | HOH937 |
| B | HOH947 |
| B | HOH1005 |
| B | HOH1037 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IPH B 802 |
| Chain | Residue |
| B | ASP54 |
| B | GLN112 |
| B | ARG265 |
| B | ILE279 |
| B | TYR289 |
| B | PRO364 |
| B | ALA366 |
| B | GLY367 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD C 801 |
| Chain | Residue |
| C | MET370 |
| C | ASN371 |
| C | SER373 |
| C | IPH802 |
| C | HOH808 |
| C | HOH869 |
| C | HOH916 |
| C | HOH1051 |
| C | HOH1069 |
| C | HOH1072 |
| C | HOH1093 |
| C | GLY14 |
| C | GLY16 |
| C | PRO17 |
| C | ALA18 |
| C | ASP42 |
| C | LYS43 |
| C | ARG44 |
| C | ASN50 |
| C | GLN52 |
| C | ALA53 |
| C | ASP54 |
| C | GLY55 |
| C | LEU142 |
| C | PRO144 |
| C | CYS224 |
| C | ASP225 |
| C | GLY226 |
| C | TYR289 |
| C | GLY356 |
| C | ASP357 |
| C | PRO364 |
| C | GLY367 |
| C | GLN368 |
| C | GLY369 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPH C 802 |
| Chain | Residue |
| C | ASP54 |
| C | GLN112 |
| C | VAL114 |
| C | ARG265 |
| C | TYR289 |
| C | PRO364 |
| C | ALA366 |
| C | GLY367 |
| C | FAD801 |
| site_id | AC7 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD D 801 |
| Chain | Residue |
| D | GLY14 |
| D | GLY16 |
| D | PRO17 |
| D | ALA18 |
| D | ASP42 |
| D | LYS43 |
| D | ARG44 |
| D | ASN50 |
| D | GLN52 |
| D | ALA53 |
| D | ASP54 |
| D | GLY55 |
| D | LEU142 |
| D | PRO144 |
| D | ASN191 |
| D | CYS224 |
| D | ASP225 |
| D | GLY226 |
| D | TYR289 |
| D | GLY356 |
| D | ASP357 |
| D | GLY367 |
| D | GLN368 |
| D | GLY369 |
| D | MET370 |
| D | ASN371 |
| D | SER373 |
| D | IPH802 |
| D | HOH807 |
| D | HOH868 |
| D | HOH921 |
| D | HOH933 |
| D | HOH935 |
| D | HOH1010 |
| D | HOH1051 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IPH D 802 |
| Chain | Residue |
| D | ASP54 |
| D | GLN112 |
| D | VAL114 |
| D | TYR289 |
| D | PRO364 |
| D | ALA366 |
| D | GLY367 |
| D | FAD801 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12925790, ECO:0000269|PubMed:9634698, ECO:0007744|PDB:1FOH, ECO:0007744|PDB:1PN0 |
| Chain | Residue | Details |
| A | ALA18 | |
| B | GLY51 | |
| B | GLY55 | |
| B | GLY118 | |
| B | VAL290 | |
| B | GLN368 | |
| C | ALA18 | |
| C | LYS43 | |
| C | GLY51 | |
| C | GLY55 | |
| C | GLY118 | |
| A | LYS43 | |
| C | VAL290 | |
| C | GLN368 | |
| D | ALA18 | |
| D | LYS43 | |
| D | GLY51 | |
| D | GLY55 | |
| D | GLY118 | |
| D | VAL290 | |
| D | GLN368 | |
| A | GLY51 | |
| A | GLY55 | |
| A | GLY118 | |
| A | VAL290 | |
| A | GLN368 | |
| B | ALA18 | |
| B | LYS43 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1FOH, ECO:0007744|PDB:1PN0 |
| Chain | Residue | Details |
| A | ALA358 | |
| B | ALA358 | |
| C | ALA358 | |
| D | ALA358 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 12427024, 11591156, 9634698 |
| Chain | Residue | Details |
| A | PRO364 | |
| A | ASP54 | |
| A | ARG281 | |
| A | TYR289 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 551 |
| Chain | Residue | Details |
| A | GLY55 | electrostatic stabiliser |
| A | GLU282 | electrostatic stabiliser |
| A | VAL290 | steric role |
| A | LYS365 | activator, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 551 |
| Chain | Residue | Details |
| B | GLY55 | electrostatic stabiliser |
| B | GLU282 | electrostatic stabiliser |
| B | VAL290 | steric role |
| B | LYS365 | activator, electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 551 |
| Chain | Residue | Details |
| C | GLY55 | electrostatic stabiliser |
| C | GLU282 | electrostatic stabiliser |
| C | VAL290 | steric role |
| C | LYS365 | activator, electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 551 |
| Chain | Residue | Details |
| D | GLY55 | electrostatic stabiliser |
| D | GLU282 | electrostatic stabiliser |
| D | VAL290 | steric role |
| D | LYS365 | activator, electrostatic stabiliser |
