Crystal structure of apo LIMK1 mutant D460N. Determined by X-ray diffraction at 2.26 Å resolution. Released 22 Jul 2026.
Explore 9Z6E in 3D Show helices and sheets RCSB PDB PDBe
9Z6E contains 29 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 | 332-334 | 3 | 1 |
| α-helix | 336-338 | 3 | |
| β-strand | 339-348 | 10 | 1 |
| β-strand | 351-358 | 8 | 1 |
| β-strand | 364-369 | 6 | 1 |
| α-helix | 375-390 | 16 | |
| β-strand | 396 | 1 | 2 |
| α-helix | 397-398 | 2 | |
| β-strand | 399-403 | 5 | 1 |
| β-strand | 410-414 | 5 | 1 |
| β-strand | 420 | 1 | 2 |
| α-helix | 421-426 | 6 | |
| α-helix | 434-453 | 20 | |
| β-strand | 456-457 | 2 | 3 |
| β-strand | 466-468 | 3 | 2 |
| β-strand | 474-476 | 3 | 2 |
| β-strand | 483-484 | 2 | 3 |
| α-helix | 518-521 | 4 | |
| α-helix | 529-544 | 16 | |
| β-strand | 555 | 1 | 4 |
| β-strand | 561 | 1 | 4 |
| α-helix | 563-569 | 7 | |
| α-helix | 575-576 | 2 | |
| α-helix | 579-586 | 8 | |
| α-helix | 591-593 | 3 | |
| α-helix | 595-596 | 2 | |
| α-helix | 597-612 | 16 | |
| α-helix | 618-632 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 332-333 | 2 | 5 |
| β-strand | 344 | 1 | 5 |
| β-strand | 353-356 | 4 | 5 |
| β-strand | 365-369 | 5 | 5 |
| α-helix | 375-388 | 14 | |
| β-strand | 396 | 1 | 6 |
| α-helix | 397-398 | 2 | |
| β-strand | 399-402 | 4 | 5 |
| β-strand | 410-414 | 5 | 5 |
| α-helix | 415-416 | 2 | |
| β-strand | 420 | 1 | 6 |
| α-helix | 421-426 | 6 | |
| α-helix | 434-453 | 20 | |
| β-strand | 456-457 | 2 | 7 |
| β-strand | 466-468 | 3 | 6 |
| β-strand | 474-476 | 3 | 6 |
| β-strand | 483-484 | 2 | 7 |
| α-helix | 513-515 | 3 | |
| α-helix | 518-521 | 4 | |
| α-helix | 529-544 | 16 | |
| β-strand | 555 | 1 | 8 |
| β-strand | 561 | 1 | 8 |
| α-helix | 563-569 | 7 | |
| α-helix | 575-576 | 2 | |
| α-helix | 579-586 | 8 | |
| α-helix | 591-593 | 3 | |
| α-helix | 595-596 | 2 | |
| α-helix | 597-613 | 17 | |
| α-helix | 618-631 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| LIM domain kinase 1 | A, B | protein | 313 | Homo sapiens | P53667 (AlphaFold model) |
>9Z6E_1 LIM domain kinase 1 (chains A, B) GRPHRIFRPSDLIHGEVLGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKV MRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSQYPWSQRVSFAKDIASG MAYLHSMNIIHRNLNSHNCLVRENKNVVVADFGLARLMVDEKTQPEGLRSLKKPDRKKRY TVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFL DRYCPPNCPPSFFPITVRCCDLDPEKRPSFVKLEHWLETLRMHLAGHLPLGPQLEQLDRG FWETYRRGESGLP
A covalent inhibitor targeting Cys-349 of LIMK1 confers selectivity over LIMK2. Patteson, J.B., Manolaridis, I., Hong, M.R. et al. J Biol Chem (2026) 302:113322-113322. DOI 10.1016/j.jbc.2026.113322 · PubMed
Other PDB entries of the same protein (UniProt P53667 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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