1CC4
PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| 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 | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A 395 |
| Chain | Residue |
| A | SER13 |
| A | LEU31 |
| A | GLU32 |
| A | ARG33 |
| A | GLN34 |
| A | ARG42 |
| A | ARG44 |
| A | ALA45 |
| A | GLY46 |
| A | VAL47 |
| A | GLN102 |
| A | VAL127 |
| A | CYS158 |
| A | ASP159 |
| A | GLY160 |
| A | GLY285 |
| A | ASP286 |
| A | ALA296 |
| A | LYS297 |
| A | GLY298 |
| A | LEU299 |
| A | ASN300 |
| A | PHB396 |
| A | HOH399 |
| A | HOH401 |
| A | HOH411 |
| A | HOH516 |
| A | HOH518 |
| A | HOH525 |
| A | HOH532 |
| A | HOH533 |
| A | ILE8 |
| A | GLY9 |
| A | GLY11 |
| A | PRO12 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PHB A 396 |
| Chain | Residue |
| A | ARG44 |
| A | TRP185 |
| A | TYR201 |
| A | SER212 |
| A | ARG214 |
| A | TYR222 |
| A | PRO293 |
| A | THR294 |
| A | ALA296 |
| A | FAD395 |
| site_id | SBS |
| Number of Residues | 5 |
| Details | SUBSTRATE BINDING SITE |
| Chain | Residue |
| A | TYR201 |
| A | SER212 |
| A | ARG214 |
| A | TYR222 |
| A | TYR385 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10025942","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10493859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2553983","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2819062","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3351945","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7520279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7628466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7756982","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9578477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9694855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P20586","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
