Crystal Structure Analysis of human ACK1. Determined by X-ray diffraction at 2.87 Å resolution. Released 10 Feb 2021.
Explore 6VQM in 3D Show helices and sheets RCSB PDB PDBe
6VQM contains 36 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 | 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 | 169-182 | 14 | |
| β-strand | 189 | 1 | 2 |
| β-strand | 192-196 | 5 | 1 |
| α-helix | 201 | 1 | |
| β-strand | 202-206 | 5 | 1 |
| β-strand | 212 | 1 | 2 |
| α-helix | 213-219 | 7 | |
| α-helix | 226-245 | 20 | |
| β-strand | 248-249 | 2 | 3 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-260 | 3 | 2 |
| β-strand | 266-268 | 3 | 2 |
| β-strand | 275-276 | 2 | 3 |
| α-helix | 277-278 | 2 | |
| β-strand | 284-285 | 2 | 4 |
| α-helix | 286-287 | 2 | |
| α-helix | 299-304 | 6 | |
| β-strand | 306-307 | 2 | 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 119-120 | 2 | 5 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-134 | 9 | 5 |
| β-strand | 139-146 | 8 | 5 |
| β-strand | 152-159 | 8 | 5 |
| α-helix | 171-182 | 12 | |
| β-strand | 189 | 1 | 6 |
| β-strand | 192-196 | 5 | 5 |
| α-helix | 201 | 1 | |
| β-strand | 202-206 | 5 | 5 |
| β-strand | 212 | 1 | 6 |
| α-helix | 213-219 | 7 | |
| α-helix | 221-223 | 3 | |
| α-helix | 226-245 | 20 | |
| β-strand | 248-249 | 2 | 7 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-260 | 3 | 6 |
| β-strand | 266-268 | 3 | 6 |
| β-strand | 275-276 | 2 | 7 |
| α-helix | 277-278 | 2 | |
| β-strand | 284-285 | 2 | 8 |
| 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 | 376-377 | 2 | |
| α-helix | 378-387 | 10 | |
| α-helix | 389-391 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activated CDC42 kinase 1 | A, B | protein | 289 | Homo sapiens | Q07912 (AlphaFold model) |
>6VQM_1 Activated CDC42 kinase 1 (chains A, B) GSAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLS QPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLL GTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVM QEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKE GERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRA
| ID | Name | Formula | Copies |
|---|---|---|---|
| R7P | 2-({4-[(3R,5S)-3,5-dimethylpiperazin-1-yl]-2-methoxyphenyl}amino)-9-methyl-5,7-… | C25 H29 N7 O2 | 2 |
Water and common crystallization additives (SO4) are not listed.
Crystal Structure Analysis of human ACK1. Seo, H.-S., Dhe-Paganon, S. To be published.
Other PDB entries of the same protein (UniProt Q07912 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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