Crystal structure of the ACVR1 (ALK2) kinase in complex with FKBP12 and the inhibitor E6201. Determined by X-ray diffraction at 1.52 Å resolution. Released 11 Sept 2019.
Explore 6I1S in 3D Show helices and sheets RCSB PDB PDBe
6I1S contains 25 α-helices and 26 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 |
|---|---|---|---|
| α-helix | 180-184 | 5 | |
| α-helix | 198-205 | 8 | |
| α-helix | 208 | 1 | |
| β-strand | 209-217 | 9 | 1 |
| β-strand | 220-227 | 8 | 1 |
| β-strand | 230-237 | 8 | 1 |
| α-helix | 239-241 | 3 | |
| α-helix | 242-254 | 13 | |
| β-strand | 262 | 1 | 2 |
| α-helix | 263-264 | 2 | |
| β-strand | 265-271 | 7 | 1 |
| β-strand | 278-284 | 7 | 1 |
| β-strand | 290 | 1 | 2 |
| α-helix | 291-297 | 7 | |
| β-strand | 300 | 1 | 3 |
| α-helix | 302-320 | 19 | |
| β-strand | 323 | 1 | 4 |
| β-strand | 329 | 1 | 4 |
| β-strand | 331-333 | 3 | 5 |
| α-helix | 339-341 | 3 | |
| β-strand | 342-344 | 3 | 2 |
| β-strand | 350-352 | 3 | 2 |
| β-strand | 359-362 | 4 | 5 |
| β-strand | 367-369 | 3 | 5 |
| α-helix | 379-381 | 3 | |
| α-helix | 384-387 | 4 | |
| α-helix | 396-415 | 20 | |
| β-strand | 418 | 1 | 3 |
| β-strand | 420 | 1 | 6 |
| β-strand | 423 | 1 | 6 |
| α-helix | 425-427 | 3 | |
| α-helix | 441-444 | 4 | |
| α-helix | 445-450 | 6 | |
| α-helix | 455-458 | 4 | |
| α-helix | 459-463 | 5 | |
| α-helix | 465-477 | 13 | |
| α-helix | 482-484 | 3 | |
| α-helix | 486-487 | 2 | |
| α-helix | 488-496 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 7 |
| α-helix | 21 | 1 | |
| β-strand | 22-31 | 10 | 7 |
| β-strand | 36-39 | 4 | 7 |
| β-strand | 47-50 | 4 | 7 |
| α-helix | 58-65 | 8 | |
| α-helix | 67-68 | 2 | |
| β-strand | 72-77 | 6 | 7 |
| α-helix | 79-81 | 3 | |
| β-strand | 88 | 1 | 8 |
| β-strand | 92 | 1 | 8 |
| β-strand | 98-107 | 10 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activin receptor type-1 | A | protein | 330 | Homo sapiens | Q04771 (AlphaFold model) |
| Peptidyl-prolyl cis-trans isomerase FKBP1A | B | protein | 109 | Homo sapiens | P62942 (AlphaFold model) |
>6I1S_1 Activin receptor type-1 (chains A) SMTTNVGDSTLADLLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQG ENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMG SLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQ CCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGL VLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTS LAKLMKECWYQNPSARLTALRIKKTLTKID
>6I1S_2 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains B) SMGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRG WEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
| ID | Name | Formula | Copies |
|---|---|---|---|
| E26 | (4~{S},5~{R},6~{Z},9~{S},10~{S},12~{E})-16-(ethylamino)-4,5-dimethyl-9,10,18-tr… | C21 H27 N O6 | 1 |
Water and common crystallization additives (SO4, EDO) are not listed.
Mutant ACVR1 Arrests Glial Cell Differentiation to Drive Tumorigenesis in Pediatric Gliomas. Fortin, J., Tian, R., Zarrabi, I. et al. Cancer Cell (2020) 37:308-323.e12. DOI 10.1016/j.ccell.2020.02.002 · PubMed
Other PDB entries of the same protein (UniProt Q04771 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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