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 |