4YKF
Crystal Structure of the Alkylhydroperoxide Reductase subunit F (AhpF) with NADH 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 | 0032991 | cellular_component | protein-containing complex |
| 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 |
| A | 0102039 | molecular_function | NADH-dependent peroxiredoxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue FAD A 601 |
| Chain | Residue |
| A | GLY219 |
| A | ASN257 |
| A | GLN288 |
| A | ALA290 |
| A | ALA321 |
| A | THR322 |
| A | GLY323 |
| A | CYS348 |
| A | ASN454 |
| A | GLY487 |
| A | ASP488 |
| A | GLY221 |
| A | LYS495 |
| A | GLN496 |
| A | ILE497 |
| A | ALA500 |
| A | HOH707 |
| A | HOH722 |
| A | HOH723 |
| A | HOH732 |
| A | HOH737 |
| A | HOH742 |
| A | PRO222 |
| A | HOH760 |
| A | ALA223 |
| A | GLY242 |
| A | GLU243 |
| A | ARG244 |
| A | GLY247 |
| A | GLN248 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue NAI A 602 |
| Chain | Residue |
| A | ILE361 |
| A | GLY362 |
| A | GLY363 |
| A | GLY364 |
| A | ASN365 |
| A | SER366 |
| A | GLU369 |
| A | LEU384 |
| A | GLU385 |
| A | PHE386 |
| A | LYS391 |
| A | ILE449 |
| A | MET467 |
| A | HOH706 |
| A | HOH733 |
| A | HOH745 |
| A | HOH748 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CD A 603 |
| Chain | Residue |
| A | HIS85 |
| A | GLU110 |
| A | HIS114 |
| A | HIS130 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | PRO453 |
| A | ASN454 |
| A | THR455 |
| A | ASN456 |
| A | TRP457 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | HIS438 |
| A | ASN439 |
| A | HOH754 |
| A | HOH785 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | GLY333 |
| A | GLU334 |
| A | ASP335 |
| A | GLN336 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | ASP393 |
| A | GLN394 |
| A | HOH774 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 608 |
| Chain | Residue |
| A | ASP473 |
| A | ALA474 |
| A | HOH716 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 609 |
| Chain | Residue |
| A | ARG357 |
| A | HIS380 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 610 |
| Chain | Residue |
| A | ILE440 |
| A | GLU441 |
| A | HOH758 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 611 |
| Chain | Residue |
| A | ARG210 |
| A | ASP211 |
| A | ARG237 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 612 |
| Chain | Residue |
| A | ARG517 |
| A | HOH777 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 613 |
| Chain | Residue |
| A | GLN413 |
| A | ARG432 |
| A | HOH729 |
| A | HOH767 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 614 |
| Chain | Residue |
| A | LYS340 |
| A | LEU352 |
| A | PHE353 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 615 |
| Chain | Residue |
| A | SER30 |
| A | ALA31 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 616 |
| Chain | Residue |
| A | ARG466 |
| A | PEG617 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 617 |
| Chain | Residue |
| A | ASN465 |
| A | THR491 |
| A | GOL616 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 618 |
| Chain | Residue |
| A | LYS354 |
| A | GLY355 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 619 |
| Chain | Residue |
| A | ASP281 |
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 | CYS345-ASN365 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 39 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
