1K0L
Pseudomonas aeruginosa phbh R220Q free of p-OHB
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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 701 |
Chain | Residue |
A | GLY81 |
A | PRO248 |
A | SER249 |
A | GLU250 |
A | HOH610 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 702 |
Chain | Residue |
A | ARG327 |
A | ALA330 |
A | ARG334 |
A | HOH597 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 703 |
Chain | Residue |
A | LYS175 |
A | ARG362 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 704 |
Chain | Residue |
A | ARG352 |
A | PRO354 |
A | ASP355 |
A | HOH525 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 705 |
Chain | Residue |
A | ARG33 |
A | GLU126 |
A | ARG128 |
A | HOH432 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 706 |
Chain | Residue |
A | ARG42 |
A | ARG44 |
A | HOH502 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 707 |
Chain | Residue |
A | ARG206 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 708 |
Chain | Residue |
A | ARG128 |
A | HIS162 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO3 A 709 |
Chain | Residue |
A | ASP131 |
A | GLN133 |
A | GLY134 |
A | HOH515 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO3 A 710 |
Chain | Residue |
A | ARG33 |
A | ARG33 |
site_id | BC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD A 395 |
Chain | Residue |
A | ILE8 |
A | GLY9 |
A | GLY11 |
A | PRO12 |
A | SER13 |
A | LEU31 |
A | GLU32 |
A | ARG33 |
A | GLN34 |
A | ARG42 |
A | ARG44 |
A | ALA45 |
A | GLN102 |
A | VAL127 |
A | CYS158 |
A | ASP159 |
A | GLY160 |
A | GLY163 |
A | ILE164 |
A | GLY285 |
A | ASP286 |
A | ALA296 |
A | GLY298 |
A | LEU299 |
A | HOH401 |
A | HOH403 |
A | HOH404 |
A | HOH407 |
A | HOH416 |
A | HOH418 |
A | HOH432 |
A | HOH441 |
A | HOH471 |
A | HOH479 |
A | HOH508 |
A | HOH526 |
A | HOH547 |
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 | SER13 | |
A | GLU32 | |
A | ARG42 | |
A | GLN102 | |
A | TYR201 | |
A | SER212 | |
A | TYR222 | |
A | PRO293 | |
A | LEU299 |
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 | 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 | TYR201 | 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 |