Structure of phosphorylated PAK1 kinase domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 Dec 2011.
Explore 3Q52 in 3D Show helices and sheets RCSB PDB PDBe
3Q52 contains 21 α-helices and 14 β-strands across 1 chain. 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 | 251-260 | 10 | |
| β-strand | 262 | 1 | 1 |
| α-helix | 266-268 | 3 | |
| β-strand | 270-278 | 9 | 1 |
| β-strand | 283-289 | 7 | 1 |
| β-strand | 295-302 | 8 | 1 |
| α-helix | 303-305 | 3 | |
| α-helix | 309-321 | 13 | |
| β-strand | 327 | 1 | 2 |
| α-helix | 328-329 | 2 | |
| β-strand | 330-336 | 7 | 1 |
| β-strand | 339-345 | 7 | 1 |
| β-strand | 351 | 1 | 2 |
| α-helix | 352-358 | 7 | |
| α-helix | 363-382 | 20 | |
| β-strand | 385-386 | 2 | 3 |
| α-helix | 392-394 | 3 | |
| β-strand | 395-397 | 3 | 2 |
| β-strand | 403-405 | 3 | 2 |
| β-strand | 412-413 | 2 | 3 |
| β-strand | 421 | 1 | 4 |
| α-helix | 428-430 | 3 | |
| α-helix | 433-437 | 5 | |
| β-strand | 441 | 1 | 4 |
| α-helix | 445-459 | 15 | |
| α-helix | 469-479 | 11 | |
| α-helix | 482-484 | 3 | |
| α-helix | 487-489 | 3 | |
| α-helix | 492-501 | 10 | |
| α-helix | 510-511 | 2 | |
| α-helix | 512-515 | 4 | |
| α-helix | 519-523 | 5 | |
| α-helix | 524-526 | 3 | |
| α-helix | 527-530 | 4 | |
| α-helix | 531-541 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase PAK 1 | A | protein | 306 | Homo sapiens | Q13153 (AlphaFold model) |
>3Q52_1 Serine/threonine-protein kinase PAK 1 (chains A) MSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQP KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIA AVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP EKLSAIFRDFLNRCLEMDVEKRGSAKELIQHQFLKIAKPLSSLTPLIAAAKEATKNNHLE HHHHHH
Structural insights into the autoactivation mechanism of p21-activated protein kinase. Wang, J., Wu, J.-W., Wang, Z.-X. Structure (2011) 19:1752-1761. DOI 10.1016/j.str.2011.10.013 · PubMed
Other PDB entries of the same protein (UniProt Q13153 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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