Crystal structure of Ack1 kinase domain with C-terminal SH3 domain. Determined by X-ray diffraction at 3.23 Å resolution. Released 6 Feb 2013.
Explore 4HZS in 3D Show helices and sheets RCSB PDB PDBe
4HZS contains 76 α-helices and 72 β-strands across 4 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 | 120 | 1 | 1 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-128 | 3 | 1 |
| β-strand | 133 | 1 | 1 |
| β-strand | 139-146 | 8 | 1 |
| β-strand | 152-159 | 8 | 1 |
| α-helix | 168-182 | 15 | |
| β-strand | 189 | 1 | 2 |
| β-strand | 192-196 | 5 | 1 |
| α-helix | 201 | 1 | |
| β-strand | 202-205 | 4 | 1 |
| β-strand | 212 | 1 | 2 |
| α-helix | 213-219 | 7 | |
| α-helix | 226-245 | 20 | |
| α-helix | 255-257 | 3 | |
| β-strand | 258-260 | 3 | 2 |
| β-strand | 266-268 | 3 | 2 |
| α-helix | 273-276 | 4 | |
| α-helix | 294-296 | 3 | |
| α-helix | 299-304 | 6 | |
| α-helix | 309-324 | 16 | |
| 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 | |
| α-helix | 389-391 | 3 | |
| β-strand | 392-394 | 3 | 3 |
| β-strand | 399 | 1 | 4 |
| β-strand | 407 | 1 | 4 |
| β-strand | 412-417 | 6 | 3 |
| β-strand | 419 | 1 | 5 |
| β-strand | 424-429 | 6 | 3 |
| β-strand | 435-439 | 5 | 3 |
| α-helix | 440-443 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 120 | 1 | 15 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-128 | 3 | 15 |
| β-strand | 133 | 1 | 15 |
| β-strand | 139-146 | 8 | 15 |
| β-strand | 152-159 | 8 | 15 |
| α-helix | 168-182 | 15 | |
| β-strand | 189 | 1 | 16 |
| β-strand | 192-196 | 5 | 15 |
| α-helix | 201 | 1 | |
| β-strand | 202-205 | 4 | 15 |
| β-strand | 211-212 | 2 | 16 |
| α-helix | 213-219 | 7 | |
| α-helix | 226-245 | 20 | |
| α-helix | 255-257 | 3 | |
| β-strand | 258-260 | 3 | 16 |
| β-strand | 266-268 | 3 | 16 |
| α-helix | 273-276 | 4 | |
| α-helix | 294-296 | 3 | |
| α-helix | 299-304 | 6 | |
| α-helix | 309-324 | 16 | |
| 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 | 378-388 | 11 | |
| α-helix | 389-391 | 3 | |
| β-strand | 392-394 | 3 | 17 |
| β-strand | 399 | 1 | 18 |
| β-strand | 407 | 1 | 18 |
| β-strand | 412-417 | 6 | 17 |
| β-strand | 419 | 1 | 14 |
| β-strand | 424-429 | 6 | 17 |
| β-strand | 435-439 | 5 | 17 |
| α-helix | 440-443 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activated CDC42 kinase 1 | A, B, C, D | protein | 341 | Homo sapiens | Q07912 (AlphaFold model) |
>4HZS_1 Activated CDC42 kinase 1 (chains A, B, C, D) GSQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMD DFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRY AVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKV PFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPR PEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDV ITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQD
Ack1: activation and regulation by allostery. Gajiwala, K.S., Maegley, K., Ferre, R. et al. PLoS One (2013) 8:e53994-e53994. DOI 10.1371/journal.pone.0053994 · PubMed
Other PDB entries of the same protein (UniProt Q07912 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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