6QYH
Structure of Apo HPAB from E.coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0009056 | biological_process | catabolic process |
A | 0010124 | biological_process | phenylacetate catabolic process |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0052881 | molecular_function | 4-hydroxyphenylacetate 3-monooxygenase activity |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0009056 | biological_process | catabolic process |
B | 0010124 | biological_process | phenylacetate catabolic process |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0052881 | molecular_function | 4-hydroxyphenylacetate 3-monooxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 601 |
Chain | Residue |
A | GLU359 |
A | HOH892 |
A | HOH903 |
A | HOH921 |
A | HOH971 |
B | HOH712 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue PGE A 602 |
Chain | Residue |
A | HOH737 |
A | HOH831 |
A | HOH883 |
B | ASN481 |
B | LYS484 |
A | ARG105 |
A | ASP314 |
A | ARG346 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue PGE A 603 |
Chain | Residue |
A | ASP338 |
A | PRO383 |
A | MET384 |
A | ALA387 |
A | ASN391 |
A | ARG395 |
A | GLN465 |
A | ARG469 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue PGE A 604 |
Chain | Residue |
A | GLN65 |
A | ASN71 |
A | TYR79 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue PEG A 605 |
Chain | Residue |
A | ASP73 |
A | LYS88 |
A | GLY126 |
A | ASN365 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue PEG A 606 |
Chain | Residue |
A | GLU359 |
B | ARG94 |
B | ASP354 |
B | CYS357 |
B | SER358 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue PEG A 607 |
Chain | Residue |
A | ASP219 |
A | HOH743 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PEG A 608 |
Chain | Residue |
A | ASP91 |
A | ARG94 |
A | GLN95 |
B | GLN65 |
B | ASN71 |
B | TYR79 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue PEG A 609 |
Chain | Residue |
A | THR41 |
B | LEU518 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue PEG A 610 |
Chain | Residue |
A | ASP511 |
B | THR41 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue CA B 601 |
Chain | Residue |
B | ASN391 |
B | GLU394 |
B | GLU455 |
B | HOH720 |
B | HOH720 |
B | HOH808 |
B | HOH808 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue CA B 602 |
Chain | Residue |
A | HOH716 |
A | HOH898 |
B | GLY26 |
B | HOH705 |
B | HOH767 |
B | HOH795 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue PGE B 603 |
Chain | Residue |
A | ASN481 |
A | LYS484 |
A | MET485 |
B | ARG105 |
B | ASP314 |
B | ARG346 |
B | HOH870 |
B | HOH898 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue PEG B 604 |
Chain | Residue |
B | GLN54 |
B | ASP57 |
B | LYS61 |
B | MET64 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EPE B 605 |
Chain | Residue |
B | TRP70 |
B | ASN71 |
B | ARG85 |
B | SER89 |
B | ASP92 |