4YKG
Crystal Structure of the Alkylhydroperoxide Reductase subunit F (AhpF) with NAD+ from Escherichia coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000302 | biological_process | response to reactive oxygen species |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0005829 | cellular_component | cytosol |
A | 0006979 | biological_process | response to oxidative stress |
A | 0008785 | molecular_function | alkyl hydroperoxide reductase activity |
A | 0009321 | cellular_component | alkyl hydroperoxide reductase complex |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0042744 | biological_process | hydrogen peroxide catabolic process |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0051287 | molecular_function | NAD binding |
A | 0071949 | molecular_function | FAD binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | binding site for residue FAD A 601 |
Chain | Residue |
A | GLY219 |
A | THR252 |
A | ASN257 |
A | GLN288 |
A | SER289 |
A | ALA290 |
A | ALA321 |
A | THR322 |
A | GLY323 |
A | CYS348 |
A | TRP457 |
A | GLY221 |
A | GLY487 |
A | ASP488 |
A | LYS495 |
A | GLN496 |
A | ILE497 |
A | HOH716 |
A | HOH723 |
A | HOH739 |
A | HOH740 |
A | HOH746 |
A | PRO222 |
A | HOH755 |
A | HOH761 |
A | HOH776 |
A | ALA223 |
A | GLY242 |
A | GLU243 |
A | ARG244 |
A | GLY247 |
A | GLN248 |
site_id | AC2 |
Number of Residues | 19 |
Details | binding site for residue NAD A 602 |
Chain | Residue |
A | GLN336 |
A | ILE361 |
A | GLY362 |
A | GLY364 |
A | ASN365 |
A | SER366 |
A | LEU384 |
A | GLU385 |
A | PHE386 |
A | LYS391 |
A | ILE449 |
A | MET467 |
A | PRO493 |
A | HOH701 |
A | HOH726 |
A | HOH731 |
A | HOH738 |
A | HOH745 |
A | HOH788 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 603 |
Chain | Residue |
A | PRO453 |
A | ASN454 |
A | THR455 |
A | ASN456 |
A | TRP457 |
A | HOH711 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 604 |
Chain | Residue |
A | HIS438 |
A | ASN439 |
A | HOH762 |
A | HOH769 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 605 |
Chain | Residue |
A | GLY333 |
A | GLU334 |
A | ASP335 |
A | GLN336 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 606 |
Chain | Residue |
A | ASP393 |
A | GLN394 |
A | HOH771 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 607 |
Chain | Residue |
A | ARG357 |
A | HIS380 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 608 |
Chain | Residue |
A | ASP473 |
A | ALA474 |
A | HOH757 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 609 |
Chain | Residue |
A | ARG327 |
A | ASN328 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 610 |
Chain | Residue |
A | GLU279 |
A | LYS354 |
A | GOL615 |
A | HOH720 |
A | HOH790 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 611 |
Chain | Residue |
A | GLU243 |
A | SER289 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CD A 612 |
Chain | Residue |
A | HIS85 |
A | GLU110 |
A | HIS130 |
A | HOH825 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 613 |
Chain | Residue |
A | LEU352 |
A | PHE353 |
A | GOL618 |
A | HOH781 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue GOL A 614 |
Chain | Residue |
A | ARG466 |
A | HOH753 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue GOL A 615 |
Chain | Residue |
A | ASP281 |
A | SO4610 |
A | HOH720 |
A | HOH742 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue GOL A 616 |
Chain | Residue |
A | GLU265 |
A | GLN413 |
A | ARG432 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue GOL A 617 |
Chain | Residue |
A | ASP278 |
A | TYR280 |
site_id | AD9 |
Number of Residues | 10 |
Details | binding site for residue GOL A 618 |
Chain | Residue |
A | THR339 |
A | LYS340 |
A | GLY341 |
A | VAL342 |
A | THR343 |
A | ASP349 |
A | LEU352 |
A | PHE353 |
A | GOL613 |
A | HOH749 |
site_id | AE1 |
Number of Residues | 7 |
Details | binding site for residue PEG A 619 |
Chain | Residue |
A | LEU2 |
A | ASP3 |
A | THR4 |
A | ILE294 |
A | GLN304 |
A | GLU306 |
A | HOH843 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue PEG A 620 |
Chain | Residue |
A | GLU206 |
A | ARG210 |
A | ASP211 |
A | ARG237 |
Functional Information from PROSITE/UniProt
site_id | PS00573 |
Number of Residues | 21 |
Details | PYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CphCDGpl..FkgkrVaVIGGGN |
Chain | Residue | Details |
A | CSD345-ASN365 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP214 | |
A | ARG357 | |
A | THR478 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS53 | |
A | LYS354 |