Structural basis for the defects of human lung cancer somatic mutations in the repression activity of Keap1 on Nrf2. Determined by X-ray diffraction at 1.6 Å resolution. Released 7 Mar 2006.
Explore 1X2J in 3D Show helices and sheets RCSB PDB PDBe
1X2J contains 7 α-helices and 42 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 | 380-383 | 4 | 3 |
| β-strand | 386-389 | 4 | 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 | 449-452 | 4 | 6 |
| α-helix | 454-456 | 3 | |
| β-strand | 461 | 1 | 7 |
| β-strand | 464-468 | 5 | 8 |
| β-strand | 471-475 | 5 | 8 |
| β-strand | 478 | 1 | 7 |
| β-strand | 483 | 1 | 7 |
| β-strand | 487-491 | 5 | 8 |
| α-helix | 492-494 | 3 | |
| β-strand | 496-500 | 5 | 8 |
| α-helix | 501-503 | 3 | |
| β-strand | 508 | 1 | 9 |
| β-strand | 511-515 | 5 | 10 |
| β-strand | 518-522 | 5 | 10 |
| β-strand | 525 | 1 | 9 |
| β-strand | 530 | 1 | 9 |
| β-strand | 534-538 | 5 | 10 |
| β-strand | 544-546 | 3 | 10 |
| α-helix | 548-550 | 3 | |
| β-strand | 555 | 1 | 11 |
| β-strand | 558-562 | 5 | 12 |
| β-strand | 565-569 | 5 | 12 |
| β-strand | 572 | 1 | 11 |
| β-strand | 577 | 1 | 11 |
| β-strand | 580-585 | 6 | 12 |
| β-strand | 590-596 | 7 | 12 |
| β-strand | 602 | 1 | 2 |
| β-strand | 605-609 | 5 | 1 |
| α-helix | 610-612 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kelch-like ECH-associated protein 1 | A | protein | 316 | Mus musculus | Q9Z2X8 (AlphaFold model) |
>1X2J_1 Kelch-like ECH-associated protein 1 (chains A) TLHKPTQAVPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSNGSWLRLADLQVPRSGLAGC VVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCASMSVPRNRIGVGVIDGHIYAV GGSHGCIHHSSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAE CYYPERNEWRMITPMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVA PMRHHRSALGITVHQGKIYVLGGYDGHTFLDSVECYDPDSDTWSEVTRMTSGRSGVGVAV TMEPCRKQIDQQNCTC
Structural basis for defects of keap1 activity provoked by its point mutations in lung cancer. Padmanabhan, B., Tong, K.I., Ohta, T. et al. Mol Cell (2006) 21:689-700. DOI 10.1016/j.molcel.2006.01.013 · 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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