Structural basis for the auto-inhibition of c-Abl tyrosine kinase. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Apr 2003.
Explore 1OPK in 3D Show helices and sheets RCSB PDB PDBe
1OPK contains 30 α-helices and 34 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 | 84-87 | 4 | 1 |
| β-strand | 91 | 1 | 2 |
| β-strand | 98 | 1 | 1 |
| β-strand | 101 | 1 | 2 |
| β-strand | 106-112 | 7 | 1 |
| β-strand | 118-122 | 5 | 1 |
| β-strand | 127-131 | 5 | 1 |
| α-helix | 132-134 | 3 | |
| β-strand | 135-137 | 3 | 1 |
| α-helix | 141-143 | 3 | |
| β-strand | 147-150 | 4 | 3 |
| α-helix | 153-159 | 7 | |
| α-helix | 160-162 | 3 | |
| β-strand | 167-172 | 6 | 3 |
| β-strand | 180-186 | 7 | 3 |
| β-strand | 189-194 | 6 | 3 |
| α-helix | 195 | 1 | |
| β-strand | 196-197 | 2 | 4 |
| β-strand | 203-204 | 2 | 4 |
| β-strand | 211 | 1 | 4 |
| α-helix | 214-221 | 8 | |
| β-strand | 226 | 1 | 5 |
| β-strand | 228 | 1 | 5 |
| β-strand | 234-235 | 2 | 3 |
| α-helix | 236-237 | 2 | |
| α-helix | 241-243 | 3 | |
| β-strand | 255 | 1 | 6 |
| α-helix | 258-260 | 3 | |
| β-strand | 261-266 | 6 | 6 |
| α-helix | 268-270 | 3 | |
| β-strand | 275-280 | 6 | 6 |
| α-helix | 281-283 | 3 | |
| β-strand | 285-291 | 7 | 6 |
| α-helix | 299-311 | 13 | |
| β-strand | 317 | 1 | 7 |
| β-strand | 320-324 | 5 | 6 |
| α-helix | 330 | 1 | |
| β-strand | 331-335 | 5 | 6 |
| β-strand | 341 | 1 | 7 |
| α-helix | 342-348 | 7 | |
| α-helix | 356-375 | 20 | |
| β-strand | 378-379 | 2 | 8 |
| α-helix | 385-387 | 3 | |
| β-strand | 388-390 | 3 | 7 |
| α-helix | 392-394 | 3 | |
| β-strand | 396-398 | 3 | 7 |
| β-strand | 404-405 | 2 | 8 |
| β-strand | 408 | 1 | 9 |
| β-strand | 410 | 1 | 9 |
| β-strand | 412-413 | 2 | 10 |
| α-helix | 414-415 | 2 | |
| α-helix | 422-424 | 3 | |
| α-helix | 427-432 | 6 | |
| β-strand | 434-435 | 2 | 10 |
| α-helix | 437-452 | 16 | |
| α-helix | 456-457 | 2 | |
| α-helix | 464-466 | 3 | |
| α-helix | 467-472 | 6 | |
| α-helix | 477-480 | 4 | |
| α-helix | 485-494 | 10 | |
| α-helix | 499-501 | 3 | |
| α-helix | 503-504 | 2 | |
| α-helix | 505-513 | 9 | |
| α-helix | 521-530 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proto-oncogene tyrosine-protein kinase ABL1 | A | protein | 495 | Mus musculus | P00520 (AlphaFold model) |
>1OPK_1 Proto-oncogene tyrosine-protein kinase ABL1 (chains A) GAMDPSEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTL SITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYL LSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVH HHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGV WKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY GNLLDYLRECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRNLAARNCLVGENHLVKVA DFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPY PGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQES SISDEVEKELGKRGT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MYR | Myristic acid | C14 H28 O2 | 1 |
| P16 | 6-(2,6-dichlorophenyl)-2-{[3-(hydroxymethyl)phenyl]amino}-8-METHYLPYRIDO[2,3-D]… | C21 H16 Cl2 N4 O2 | 1 |
Water and common crystallization additives (GOL) 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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