Crystal Structure of Ack1 with compound T95. Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Dec 2008.
Explore 3EQP in 3D Show helices and sheets RCSB PDB PDBe
3EQP contains 40 α-helices and 28 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 | 119-120 | 2 | 5 |
| β-strand | 126-135 | 10 | 5 |
| β-strand | 138-146 | 9 | 5 |
| β-strand | 152-159 | 8 | 5 |
| α-helix | 168-182 | 15 | |
| β-strand | 189 | 1 | 6 |
| α-helix | 190-191 | 2 | |
| β-strand | 192-196 | 5 | 5 |
| α-helix | 201 | 1 | |
| β-strand | 202-206 | 5 | 5 |
| β-strand | 211-212 | 2 | 6 |
| α-helix | 213-220 | 8 | |
| α-helix | 221-223 | 3 | |
| α-helix | 226-245 | 20 | |
| β-strand | 248-249 | 2 | 7 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-262 | 5 | 6 |
| β-strand | 265-268 | 4 | 6 |
| β-strand | 275-276 | 2 | 7 |
| α-helix | 277-278 | 2 | |
| β-strand | 284-285 | 2 | 8 |
| α-helix | 294-296 | 3 | |
| α-helix | 299-304 | 6 | |
| β-strand | 306-307 | 2 | 8 |
| α-helix | 309-324 | 16 | |
| α-helix | 328-329 | 2 | |
| α-helix | 336-340 | 5 | |
| α-helix | 341-345 | 5 | |
| α-helix | 350-353 | 4 | |
| α-helix | 358-367 | 10 | |
| α-helix | 372-374 | 3 | |
| α-helix | 376-377 | 2 | |
| α-helix | 378-387 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 119-120 | 2 | 1 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-135 | 10 | 1 |
| β-strand | 138-146 | 9 | 1 |
| β-strand | 152-159 | 8 | 1 |
| α-helix | 168-183 | 16 | |
| β-strand | 189 | 1 | 2 |
| α-helix | 190-191 | 2 | |
| β-strand | 192-196 | 5 | 1 |
| α-helix | 201 | 1 | |
| β-strand | 202-206 | 5 | 1 |
| β-strand | 212 | 1 | 2 |
| α-helix | 213-217 | 5 | |
| α-helix | 221-223 | 3 | |
| α-helix | 226-245 | 20 | |
| β-strand | 248-249 | 2 | 3 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-262 | 5 | 2 |
| β-strand | 265-268 | 4 | 2 |
| β-strand | 275-276 | 2 | 3 |
| β-strand | 283-285 | 3 | 4 |
| α-helix | 286-287 | 2 | |
| α-helix | 288-290 | 3 | |
| α-helix | 294-296 | 3 | |
| α-helix | 299-304 | 6 | |
| β-strand | 306-308 | 3 | 4 |
| α-helix | 309-324 | 16 | |
| α-helix | 328-329 | 2 | |
| α-helix | 336-340 | 5 | |
| α-helix | 341-345 | 5 | |
| α-helix | 350-353 | 4 | |
| α-helix | 358-367 | 10 | |
| α-helix | 372-374 | 3 | |
| α-helix | 376-377 | 2 | |
| α-helix | 378-387 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activated CDC42 kinase 1 | A, B | protein | 276 | Homo sapiens | Q07912 (AlphaFold model) |
>3EQP_1 Activated CDC42 kinase 1 (chains A, B) LTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIR EVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQV AEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAW CAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDC PQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTD
| ID | Name | Formula | Copies |
|---|---|---|---|
| T95 | N-(2,6-dimethylphenyl)-4-(2-ethoxyphenoxy)-2-({4-[4-(2-hydroxyethyl)piperazin-1… | C33 H38 N6 O4 | 2 |
Water and common crystallization additives (CL) are not listed.
Identification and optimization of N3,N6-diaryl-1H-pyrazolo[3,4-d]pyrimidine-3,6-diamines as a novel class of ACK1 inhibitors. Kopecky, D.J., Hao, X., Chen, Y. et al. Bioorg Med Chem Lett (2008) 18:6352-6356. DOI 10.1016/j.bmcl.2008.10.092 · PubMed
Other PDB entries of the same protein (UniProt Q07912 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3EQP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.