ABL kinase in complex with imatinib and a fragment (FRAG1) in the myristate pocket. Determined by X-ray diffraction at 1.8 Å resolution. Released 26 May 2010.
Explore 3MS9 in 3D Show helices and sheets RCSB PDB PDBe
3MS9 contains 44 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 | 236 | 1 | 1 |
| α-helix | 239-241 | 3 | |
| β-strand | 242-247 | 6 | 1 |
| α-helix | 248-251 | 4 | |
| β-strand | 256-261 | 6 | 1 |
| α-helix | 262-264 | 3 | |
| β-strand | 266-272 | 7 | 1 |
| α-helix | 281-291 | 11 | |
| β-strand | 298 | 1 | 2 |
| α-helix | 299-300 | 2 | |
| β-strand | 301-305 | 5 | 1 |
| α-helix | 311 | 1 | |
| β-strand | 312-316 | 5 | 1 |
| β-strand | 321-322 | 2 | 2 |
| α-helix | 323-329 | 7 | |
| α-helix | 337-356 | 20 | |
| α-helix | 366-368 | 3 | |
| β-strand | 369-371 | 3 | 2 |
| α-helix | 373-375 | 3 | |
| β-strand | 377-379 | 3 | 2 |
| α-helix | 384-386 | 3 | |
| β-strand | 394-396 | 3 | 3 |
| β-strand | 399-401 | 3 | 3 |
| α-helix | 403-405 | 3 | |
| α-helix | 408-413 | 6 | |
| α-helix | 418-433 | 16 | |
| α-helix | 437-438 | 2 | |
| α-helix | 445-447 | 3 | |
| α-helix | 448-453 | 6 | |
| α-helix | 458-461 | 4 | |
| α-helix | 466-475 | 10 | |
| α-helix | 480-482 | 3 | |
| α-helix | 484-485 | 2 | |
| α-helix | 486-497 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 236 | 1 | 4 |
| α-helix | 239-241 | 3 | |
| β-strand | 242-247 | 6 | 4 |
| α-helix | 248-251 | 4 | |
| β-strand | 256-261 | 6 | 4 |
| α-helix | 262-264 | 3 | |
| β-strand | 266-272 | 7 | 4 |
| α-helix | 280-291 | 12 | |
| β-strand | 298 | 1 | 5 |
| α-helix | 299-300 | 2 | |
| β-strand | 301-305 | 5 | 4 |
| α-helix | 311 | 1 | |
| β-strand | 312-316 | 5 | 4 |
| β-strand | 322 | 1 | 5 |
| α-helix | 323-329 | 7 | |
| α-helix | 337-356 | 20 | |
| α-helix | 366-368 | 3 | |
| β-strand | 369-371 | 3 | 5 |
| α-helix | 373-375 | 3 | |
| β-strand | 377-379 | 3 | 5 |
| α-helix | 384-386 | 3 | |
| β-strand | 394-396 | 3 | 6 |
| β-strand | 399-401 | 3 | 6 |
| α-helix | 403-405 | 3 | |
| α-helix | 408-413 | 6 | |
| α-helix | 418-433 | 16 | |
| α-helix | 437-438 | 2 | |
| α-helix | 445-447 | 3 | |
| α-helix | 448-453 | 6 | |
| α-helix | 458-461 | 4 | |
| α-helix | 466-475 | 10 | |
| α-helix | 480-482 | 3 | |
| α-helix | 484-485 | 2 | |
| α-helix | 486-497 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tyrosine-protein kinase ABL1 | A, B | protein | 293 | Mus musculus | P00520 (AlphaFold model) |
>3MS9_1 Tyrosine-protein kinase ABL1 (chains A, B) GAMDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEE FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLY MATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFP IKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPE GCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKRGT
| ID | Name | Formula | Copies |
|---|---|---|---|
| MS9 | methyl 2-amino-4-chlorobenzoate | C8 H8 Cl N 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.
Binding or bending: distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay. Jahnke, W., Grotzfeld, R.M., Pelle, X. et al. J Am Chem Soc (2010) 132:7043-7048. DOI 10.1021/ja101837n · 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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