Structure and regulation of the CDK5-p25(nck5a) complex. Determined by X-ray diffraction at 2.65 Å resolution. Released 14 Aug 2002.
Explore 1H4L in 3D Show helices and sheets RCSB PDB PDBe
1H4L contains 43 α-helices and 24 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 | 5-6 | 2 | 1 |
| β-strand | 19-22 | 4 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-36 | 2 | 1 |
| α-helix | 44-55 | 12 | |
| β-strand | 60 | 1 | 2 |
| β-strand | 63 | 1 | 2 |
| β-strand | 66-72 | 7 | 1 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 85-86 | 2 | 2 |
| α-helix | 87-93 | 7 | |
| 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 |
| α-helix | 145-147 | 3 | |
| β-strand | 149-150 | 2 | 3 |
| α-helix | 165-167 | 3 | |
| α-helix | 170-173 | 4 | |
| α-helix | 182-195 | 14 | |
| α-helix | 208-219 | 12 | |
| α-helix | 228-232 | 5 | |
| α-helix | 248-251 | 4 | |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-281 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 4 |
| β-strand | 18-22 | 5 | 4 |
| β-strand | 29-36 | 8 | 4 |
| α-helix | 44-56 | 13 | |
| β-strand | 63 | 1 | 5 |
| β-strand | 66-71 | 6 | 4 |
| β-strand | 75-81 | 7 | 4 |
| α-helix | 82 | 1 | |
| β-strand | 85-86 | 2 | 5 |
| α-helix | 87-93 | 7 | |
| 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 |
| α-helix | 145-147 | 3 | |
| 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 | 248-250 | 3 | |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-276 | 3 | |
| α-helix | 277-281 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 148-162 | 15 | |
| α-helix | 172-184 | 13 | |
| α-helix | 198-211 | 14 | |
| α-helix | 219-237 | 19 | |
| α-helix | 254-277 | 24 | |
| α-helix | 279-290 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 148-162 | 15 | |
| α-helix | 172-186 | 15 | |
| α-helix | 198-211 | 14 | |
| α-helix | 219-237 | 19 | |
| α-helix | 254-277 | 24 | |
| α-helix | 279-291 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division protein kinase 5 | A, B | protein | 292 | HOMO SAPIENS | Q00535 (AlphaFold model) |
| Cyclin-dependent kinase 5 activator | D, E | protein | 147 | HOMO SAPIENS | Q15078 (AlphaFold model) |
>1H4L_1 CELL DIVISION PROTEIN KINASE 5 (chains A, B) MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKH KNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSR NVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYS TSIDMWSAGCIFAELANAARPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYP MYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP
>1H4L_2 CYCLIN-DEPENDENT KINASE 5 ACTIVATOR (chains D, E) STSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYM LCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVIN LMSSKMLQINADPHYFTQVFSDLKNES
Structure and Regulation of the Cdk5-P25(Nck5A) Complex. Tarricone, C., Dhavan, R., Peng, J. et al. Mol Cell (2001) 8:657. DOI 10.1016/S1097-2765(01)00343-4 · 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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