1BF3
P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 42 REPLACED BY LYS (R42K), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID
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 | 0018659 | molecular_function | 4-hydroxybenzoate 3-monooxygenase activity |
A | 0043639 | biological_process | benzoate catabolic process |
A | 0043640 | biological_process | benzoate catabolic process via hydroxylation |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071949 | molecular_function | FAD binding |
A | 0106356 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADPH) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 395 |
Chain | Residue |
A | GLY9 |
A | ALA45 |
A | GLY46 |
A | VAL47 |
A | GLN102 |
A | CYS158 |
A | ASP159 |
A | GLY160 |
A | GLY285 |
A | ASP286 |
A | ALA296 |
A | GLY11 |
A | LYS297 |
A | GLY298 |
A | LEU299 |
A | ASN300 |
A | PHB396 |
A | HOH400 |
A | HOH402 |
A | HOH411 |
A | HOH521 |
A | HOH523 |
A | PRO12 |
A | HOH530 |
A | HOH537 |
A | HOH645 |
A | SER13 |
A | LEU31 |
A | GLU32 |
A | ARG33 |
A | GLN34 |
A | ARG44 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PHB A 396 |
Chain | Residue |
A | ARG44 |
A | VAL47 |
A | TRP185 |
A | TYR201 |
A | SER212 |
A | ARG214 |
A | TYR222 |
A | PRO293 |
A | THR294 |
A | FAD395 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855 |
Chain | Residue | Details |
A | SER13 | |
A | LEU299 | |
A | GLU32 | |
A | LYS42 | |
A | GLN102 | |
A | TYR201 | |
A | SER212 | |
A | TYR222 | |
A | ASP286 | |
A | PRO293 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P20586 |
Chain | Residue | Details |
A | TYR201 | |
A | TYR385 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dod |
Chain | Residue | Details |
A | TYR201 | |
A | TYR385 |