Crystal structure of compound 4a in complex with cdk5, showing an unusual binding mode to the hinge region via a water molecule. Determined by X-ray diffraction at 1.9 Å resolution. Released 27 Mar 2013.
Explore 4AU8 in 3D Show helices and sheets RCSB PDB PDBe
4AU8 contains 37 α-helices and 23 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 |
|---|---|---|---|
| α-helix | 1-3 | 3 | |
| β-strand | 4-12 | 9 | 1 |
| β-strand | 17-23 | 7 | 1 |
| β-strand | 29-34 | 6 | 1 |
| α-helix | 46-55 | 10 | |
| β-strand | 63 | 1 | 2 |
| β-strand | 66-70 | 5 | 1 |
| β-strand | 77-81 | 5 | 1 |
| β-strand | 85-86 | 2 | 2 |
| α-helix | 87-94 | 8 | |
| α-helix | 100-119 | 20 | |
| β-strand | 122-123 | 2 | 3 |
| α-helix | 129-131 | 3 | |
| β-strand | 132-134 | 3 | 2 |
| β-strand | 140-142 | 3 | 2 |
| β-strand | 149-150 | 2 | 3 |
| β-strand | 153 | 1 | 3 |
| α-helix | 165-167 | 3 | |
| α-helix | 170-173 | 4 | |
| α-helix | 182-196 | 15 | |
| α-helix | 208-219 | 12 | |
| α-helix | 221-223 | 3 | |
| α-helix | 228-232 | 5 | |
| α-helix | 238-240 | 3 | |
| α-helix | 242-245 | 4 | |
| α-helix | 248-250 | 3 | |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-281 | 5 | |
| α-helix | 284-286 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 4 |
| β-strand | 17-23 | 7 | 4 |
| β-strand | 29-36 | 8 | 4 |
| α-helix | 43-55 | 13 | |
| β-strand | 63 | 1 | 5 |
| β-strand | 66-71 | 6 | 4 |
| β-strand | 75-80 | 6 | 4 |
| β-strand | 85-86 | 2 | 5 |
| α-helix | 87-92 | 6 | |
| α-helix | 100-119 | 20 | |
| β-strand | 122-123 | 2 | 6 |
| α-helix | 129-131 | 3 | |
| β-strand | 132-134 | 3 | 5 |
| β-strand | 140-142 | 3 | 5 |
| β-strand | 149-150 | 2 | 6 |
| α-helix | 165-167 | 3 | |
| α-helix | 170-173 | 4 | |
| α-helix | 182-196 | 15 | |
| α-helix | 208-219 | 12 | |
| α-helix | 221-223 | 3 | |
| α-helix | 228-232 | 5 | |
| α-helix | 238-240 | 3 | |
| α-helix | 242-245 | 4 | |
| α-helix | 248-250 | 3 | |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-281 | 5 | |
| α-helix | 284-286 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 5 | A, B | protein | 296 | HOMO SAPIENS | Q00535 (AlphaFold model) |
>4AU8_1 CYCLIN-DEPENDENT KINASE 5 (chains A, B) GAMGSQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLK ELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGF CHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGA KLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDY KPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP
| ID | Name | Formula | Copies |
|---|---|---|---|
| Z3R | 4-(1,3-benzothiazol-2-yl)thiophene-2-sulfonamide | C11 H8 N2 O2 S3 | 2 |
Water and common crystallization additives (IMD, SO4) are not listed.
Synthesis and Structure-Activity Relationship of 4-(1,3-Benzothiazol-2-Yl)-Thiophene-2-Sulfonamides as Cyclin-Dependent Kinase 5 (Cdk5)/P25 Inhibitors. Malmstrom, J., Viklund, J., Slivo, C. et al. Bioorg Med Chem Lett (2012) 22:5919. DOI 10.1016/J.BMCL.2012.07.068 · PubMed
Other PDB entries of the same protein (UniProt Q00535 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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