Structural basis for the auto-inhibition of c-Abl tyrosine kinase. Determined by X-ray diffraction at 1.75 Å resolution. Released 8 Apr 2003.
Explore 1OPJ in 3D Show helices and sheets RCSB PDB PDBe
1OPJ contains 43 α-helices and 24 β-strands across 2 chains. 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 | 255 | 1 | 1 |
| α-helix | 258-260 | 3 | |
| β-strand | 261-266 | 6 | 1 |
| β-strand | 275-280 | 6 | 1 |
| α-helix | 281-283 | 3 | |
| β-strand | 285-291 | 7 | 1 |
| α-helix | 292-293 | 2 | |
| α-helix | 299-311 | 13 | |
| β-strand | 317 | 1 | 2 |
| α-helix | 318-319 | 2 | |
| β-strand | 320-324 | 5 | 1 |
| α-helix | 330 | 1 | |
| β-strand | 331-335 | 5 | 1 |
| β-strand | 341 | 1 | 2 |
| α-helix | 342-348 | 7 | |
| α-helix | 356-375 | 20 | |
| α-helix | 385-387 | 3 | |
| β-strand | 388-390 | 3 | 2 |
| α-helix | 392-394 | 3 | |
| β-strand | 396-398 | 3 | 2 |
| β-strand | 413-415 | 3 | 3 |
| β-strand | 418-420 | 3 | 3 |
| α-helix | 422-424 | 3 | |
| α-helix | 427-432 | 6 | |
| α-helix | 437-452 | 16 | |
| α-helix | 456-457 | 2 | |
| α-helix | 464-472 | 9 | |
| α-helix | 477-480 | 4 | |
| α-helix | 485-494 | 10 | |
| α-helix | 499-501 | 3 | |
| α-helix | 503-504 | 2 | |
| α-helix | 505-514 | 10 | |
| α-helix | 521-528 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 255 | 1 | 4 |
| α-helix | 258-260 | 3 | |
| β-strand | 262-266 | 5 | 4 |
| α-helix | 267-270 | 4 | |
| β-strand | 275-280 | 6 | 4 |
| α-helix | 281-283 | 3 | |
| β-strand | 285-290 | 6 | 4 |
| α-helix | 299-311 | 13 | |
| β-strand | 317 | 1 | 5 |
| α-helix | 318-319 | 2 | |
| β-strand | 320-324 | 5 | 4 |
| α-helix | 330 | 1 | |
| β-strand | 331-335 | 5 | 4 |
| α-helix | 336-337 | 2 | |
| β-strand | 341 | 1 | 5 |
| α-helix | 342-348 | 7 | |
| α-helix | 356-375 | 20 | |
| α-helix | 385-387 | 3 | |
| β-strand | 388-390 | 3 | 5 |
| α-helix | 392-394 | 3 | |
| β-strand | 396-398 | 3 | 5 |
| β-strand | 413-415 | 3 | 6 |
| β-strand | 418-420 | 3 | 6 |
| α-helix | 422-424 | 3 | |
| α-helix | 427-432 | 6 | |
| α-helix | 437-452 | 16 | |
| α-helix | 456-457 | 2 | |
| α-helix | 464-472 | 9 | |
| α-helix | 477-480 | 4 | |
| α-helix | 485-494 | 10 | |
| α-helix | 499-501 | 3 | |
| α-helix | 503-504 | 2 | |
| α-helix | 505-512 | 8 | |
| α-helix | 521-529 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proto-oncogene tyrosine-protein kinase ABL1 | A, B | protein | 293 | Mus musculus | P00520 (AlphaFold model) |
>1OPJ_1 Proto-oncogene tyrosine-protein kinase ABL1 (chains A, B) GAMDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEE FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLY MATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFP IKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPE GCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKRGT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MYR | Myristic acid | C14 H28 O2 | 2 |
| STI | 4-(4-methyl-piperazin-1-ylmethyl)-N-[4-methyl-3-(4-pyridin-3-yl-pyrimidin-2-yla… | C29 H31 N7 O | 2 |
Water and common crystallization additives (CL) are not listed.
Structural basis for the autoinhibition of c-Abl tyrosine kinase. Nagar, B., Hantschel, O., Young, M.A. et al. Cell (2003) 112:859-871. DOI 10.1016/S0092-8674(03)00194-6 · PubMed
Other PDB entries of the same protein (UniProt P00520 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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