1PBC
CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0009056 | biological_process | catabolic process |
| 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 | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 395 |
| Chain | Residue |
| A | ILE8 |
| A | ALA45 |
| A | GLN102 |
| A | CYS158 |
| A | ASP159 |
| A | GLY160 |
| A | GLY163 |
| A | ILE164 |
| A | TYR222 |
| A | GLY285 |
| A | ASP286 |
| A | GLY9 |
| A | GLY298 |
| A | LEU299 |
| A | BHA396 |
| A | HOH399 |
| A | HOH408 |
| A | HOH516 |
| A | HOH525 |
| A | HOH529 |
| A | HOH583 |
| A | HOH602 |
| A | GLY11 |
| A | PRO12 |
| A | SER13 |
| A | GLU32 |
| A | ARG33 |
| A | ARG42 |
| A | ARG44 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BHA A 396 |
| Chain | Residue |
| A | VAL47 |
| A | TRP185 |
| A | LEU199 |
| A | TYR201 |
| A | LEU210 |
| A | SER212 |
| A | ARG214 |
| A | TYR222 |
| A | PRO293 |
| A | THR294 |
| A | ALA296 |
| 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 | ARG42 | |
| 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 |
