6JU1
p-Hydroxybenzoate hydroxylase Y385F mutant complexed with 3,4-dihydroxybenzoate
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 | 37 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | GLY9 |
| A | ARG44 |
| A | ALA45 |
| A | GLY46 |
| A | VAL47 |
| A | GLN102 |
| A | VAL127 |
| A | CYS158 |
| A | ASP159 |
| A | GLY160 |
| A | GLY163 |
| A | GLY11 |
| A | GLY285 |
| A | ASP286 |
| A | ALA296 |
| A | LYS297 |
| A | GLY298 |
| A | LEU299 |
| A | ASN300 |
| A | DHB402 |
| A | BR409 |
| A | HOH571 |
| A | PRO12 |
| A | HOH615 |
| A | HOH616 |
| A | HOH625 |
| A | HOH628 |
| A | HOH651 |
| A | HOH667 |
| A | HOH676 |
| A | HOH688 |
| A | SER13 |
| A | GLU32 |
| A | ARG33 |
| A | GLN34 |
| A | VAL39 |
| A | ARG42 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue DHB A 402 |
| Chain | Residue |
| A | GLY46 |
| A | VAL47 |
| A | LEU199 |
| A | TYR201 |
| A | LEU210 |
| A | SER212 |
| A | ARG214 |
| A | ARG220 |
| A | TYR222 |
| A | PRO293 |
| A | THR294 |
| A | ALA296 |
| A | FAD401 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | ARG341 |
| A | TRP345 |
| A | TYR371 |
| A | THR380 |
| A | ILE381 |
| A | ASN384 |
| A | HOH505 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | GLU49 |
| A | GLN50 |
| A | GLY51 |
| A | LYS95 |
| A | ARG335 |
| A | VAL386 |
| A | GLY387 |
| A | TYR390 |
| A | HOH542 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 A 407 |
| Chain | Residue |
| A | HOH502 |
| A | HOH502 |
| A | HOH536 |
| A | HOH536 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue P33 A 408 |
| Chain | Residue |
| A | TRP344 |
| A | TRP344 |
| A | TRP345 |
| A | SER348 |
| A | SER348 |
| A | VAL349 |
| A | PHE353 |
| A | PHE353 |
| A | GLN364 |
| A | GLU367 |
| A | HOH601 |
| A | HOH601 |
| A | HOH801 |
| A | HOH801 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue BR A 409 |
| Chain | Residue |
| A | PRO293 |
| A | LYS297 |
| A | GLY298 |
| A | FAD401 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue BR A 410 |
| Chain | Residue |
| A | ILE43 |
| A | ALA45 |
| A | GLN102 |
| A | THR103 |
| A | ARG214 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| site_id | AD2 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| site_id | AD3 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| site_id | AD4 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| site_id | AD5 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
| site_id | AD7 |
| Number of Residues | 16 |
| Details | binding site for residues GOL A 403 and GOL A 404 |
| Chain | Residue |
| A | ARG166 |
| A | ARG166 |
| A | GLN167 |
| A | GLN167 |
| A | PRO170 |
| A | PRO170 |
| A | ALA171 |
| A | ALA171 |
| A | GLU178 |
| A | GLU178 |
| A | PHE271 |
| A | PHE271 |
| A | HOH530 |
| A | HOH530 |
| A | HOH557 |
| A | HOH635 |
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 | TYR201 | |
| 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 | TYR201 | |
| A | PHE385 |
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 | TYR201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | LYS297 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | PHE385 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | PRO293 | electrostatic stabiliser, hydrogen bond acceptor |
