1PXB
CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS
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 | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| 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 | 31 |
| Details | BINDING SITE FOR RESIDUE FAD A 395 |
| Chain | Residue |
| A | GLY9 |
| A | GLY46 |
| A | VAL47 |
| A | GLN102 |
| A | CYS158 |
| A | ASP159 |
| A | GLY163 |
| A | ILE164 |
| A | GLY285 |
| A | ASP286 |
| A | ALA296 |
| A | GLY11 |
| A | LYS297 |
| A | GLY298 |
| A | LEU299 |
| A | ASN300 |
| A | PHB396 |
| A | HOH416 |
| A | HOH455 |
| A | HOH476 |
| A | HOH477 |
| A | HOH483 |
| A | PRO12 |
| A | HOH484 |
| A | HOH497 |
| A | SER13 |
| A | GLU32 |
| A | ARG33 |
| A | ARG42 |
| A | ARG44 |
| A | ALA45 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PHB A 396 |
| Chain | Residue |
| A | ARG44 |
| A | GLY46 |
| 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 | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 |
| Chain | Residue | Details |
| A | ARG42 | |
| A | GLN102 | |
| A | PHE201 | |
| A | SER212 | |
| A | TYR222 | |
| A | PRO293 | |
| A | LEU299 | |
| A | SER13 | |
| A | GLU32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229 |
| Chain | Residue | Details |
| A | ASP286 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000269|PubMed:8312276 |
| Chain | Residue | Details |
| A | PHE201 | |
| A | TYR385 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 131 |
| Chain | Residue | Details |
| A | HIS72 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | PHE201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | PRO293 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS297 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | TYR385 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
