Crystal structure of the Keap1 protein in complexed with the N-terminal region of the Nrf2 transcription factor. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Sept 2007.
Explore 2DYH in 3D Show helices and sheets RCSB PDB PDBe
2DYH contains 6 α-helices and 41 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 327-331 | 5 | 1 |
| β-strand | 334-335 | 2 | 2 |
| β-strand | 337-338 | 2 | 2 |
| β-strand | 342-345 | 4 | 1 |
| β-strand | 352-354 | 3 | 1 |
| α-helix | 356-358 | 3 | |
| β-strand | 363 | 1 | 3 |
| β-strand | 366-370 | 5 | 4 |
| β-strand | 373-377 | 5 | 4 |
| β-strand | 380-381 | 2 | 3 |
| β-strand | 388-389 | 2 | 3 |
| β-strand | 393-397 | 5 | 4 |
| β-strand | 402-405 | 4 | 4 |
| α-helix | 407-409 | 3 | |
| β-strand | 414 | 1 | 5 |
| β-strand | 417-421 | 5 | 6 |
| β-strand | 424-428 | 5 | 6 |
| β-strand | 431-432 | 2 | 5 |
| β-strand | 435-436 | 2 | 5 |
| β-strand | 440-444 | 5 | 6 |
| β-strand | 449-453 | 5 | 6 |
| α-helix | 454-456 | 3 | |
| β-strand | 461 | 1 | 7 |
| β-strand | 464-468 | 5 | 7 |
| β-strand | 471-478 | 8 | 7 |
| β-strand | 483-491 | 9 | 7 |
| α-helix | 492-494 | 3 | |
| β-strand | 496-500 | 5 | 7 |
| α-helix | 501-503 | 3 | |
| β-strand | 508 | 1 | 8 |
| β-strand | 511-515 | 5 | 9 |
| β-strand | 518-522 | 5 | 9 |
| β-strand | 525 | 1 | 8 |
| β-strand | 530 | 1 | 8 |
| β-strand | 534-538 | 5 | 9 |
| β-strand | 543-546 | 4 | 9 |
| α-helix | 548-550 | 3 | |
| β-strand | 555 | 1 | 10 |
| β-strand | 558-562 | 5 | 11 |
| β-strand | 565-569 | 5 | 11 |
| β-strand | 572 | 1 | 10 |
| β-strand | 577 | 1 | 10 |
| β-strand | 580-585 | 6 | 11 |
| β-strand | 590-596 | 7 | 11 |
| β-strand | 602 | 1 | 2 |
| β-strand | 605-609 | 5 | 1 |
| β-strand | 616-617 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kelch-like ECH-associated protein 1 | A | protein | 318 | Mus musculus | Q9Z2X8 (AlphaFold model) |
| Nrf2/Neh2 peptide from Nuclear factor erythroid 2-related factor 2 | B | protein | 15 | Q60795 (AlphaFold model) |
>2DYH_1 Kelch-like ECH-associated protein 1 (chains A) MTLHKPTQAVPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSNGSWLRLADLQVPRSGLAG CVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCASMSVPRNRIGVGVIDGHIYA VGGSHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSA ECYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFV APMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWSEVTRMTSGRSGVGVA VTMEPCRKQIDQQNCTCY
>2DYH_2 Nrf2/Neh2 peptide from Nuclear factor erythroid 2-related factor 2 (chains B) ILWRQDIDLGVSREV
Different electrostatic potentials define ETGE and DLG motifs as hinge and latch in oxidative stress response. Tong, K.I., Padmanabhan, B., Kobayashi, A. et al. Mol Cell Biol (2007) 27:7511-7521. DOI 10.1128/MCB.00753-07 · PubMed
Other PDB entries of the same protein (UniProt Q9Z2X8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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