Structure of CDK2 in complex with cyclin A and a 2-amino-4-heteroaryl- pyrimidine inhibitor. Determined by X-ray diffraction at 2.05 Å resolution. Released 6 Mar 2013.
Explore 4BCK in 3D Show helices and sheets RCSB PDB PDBe
4BCK contains 74 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 | 4-12 | 9 | 1 |
| β-strand | 16-23 | 8 | 1 |
| β-strand | 29-36 | 8 | 1 |
| α-helix | 46-55 | 10 | |
| β-strand | 63 | 1 | 2 |
| β-strand | 66-70 | 5 | 1 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 85-86 | 2 | 2 |
| α-helix | 87-93 | 7 | |
| α-helix | 101-120 | 20 | |
| β-strand | 123-124 | 2 | 3 |
| α-helix | 130-132 | 3 | |
| β-strand | 133-135 | 3 | 2 |
| β-strand | 141-143 | 3 | 2 |
| β-strand | 150-151 | 2 | 3 |
| α-helix | 166-168 | 3 | |
| α-helix | 171-174 | 4 | |
| α-helix | 183-198 | 16 | |
| α-helix | 208-219 | 12 | |
| α-helix | 230-232 | 3 | |
| α-helix | 243-245 | 3 | |
| α-helix | 248-251 | 4 | |
| α-helix | 257-266 | 10 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-280 | 4 | |
| α-helix | 284-286 | 3 | |
| α-helix | 292-294 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 179-192 | 14 | |
| α-helix | 194-196 | 3 | |
| α-helix | 200-202 | 3 | |
| α-helix | 208-224 | 17 | |
| α-helix | 229-243 | 15 | |
| α-helix | 253-268 | 16 | |
| α-helix | 272-274 | 3 | |
| α-helix | 275-281 | 7 | |
| α-helix | 288-301 | 14 | |
| α-helix | 311-318 | 8 | |
| α-helix | 319-321 | 3 | |
| α-helix | 327-339 | 13 | |
| α-helix | 344-347 | 4 | |
| α-helix | 352-368 | 17 | |
| α-helix | 374-380 | 7 | |
| α-helix | 384-399 | 16 | |
| α-helix | 401-403 | 3 | |
| α-helix | 408-412 | 5 | |
| α-helix | 416-418 | 3 | |
| α-helix | 421-423 | 3 | |
| α-helix | 425-427 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-11 | 8 | 4 |
| β-strand | 16-23 | 8 | 4 |
| β-strand | 29-36 | 8 | 4 |
| β-strand | 38 | 1 | 5 |
| β-strand | 43 | 1 | 5 |
| α-helix | 46-57 | 12 | |
| β-strand | 63 | 1 | 6 |
| α-helix | 64-65 | 2 | |
| β-strand | 66-71 | 6 | 4 |
| β-strand | 75-81 | 7 | 4 |
| β-strand | 85-86 | 2 | 6 |
| α-helix | 87-93 | 7 | |
| α-helix | 101-120 | 20 | |
| β-strand | 123-124 | 2 | 7 |
| α-helix | 130-132 | 3 | |
| β-strand | 133-135 | 3 | 6 |
| β-strand | 141-143 | 3 | 6 |
| β-strand | 150-151 | 2 | 7 |
| α-helix | 166-168 | 3 | |
| α-helix | 171-174 | 4 | |
| α-helix | 183-198 | 16 | |
| α-helix | 208-219 | 12 | |
| α-helix | 230-232 | 3 | |
| α-helix | 243-245 | 3 | |
| α-helix | 248-251 | 4 | |
| α-helix | 257-265 | 9 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-280 | 4 | |
| α-helix | 284-286 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 179-189 | 11 | |
| α-helix | 194-196 | 3 | |
| α-helix | 199-202 | 4 | |
| α-helix | 208-224 | 17 | |
| α-helix | 229-243 | 15 | |
| α-helix | 250-252 | 3 | |
| α-helix | 253-268 | 16 | |
| α-helix | 272-274 | 3 | |
| α-helix | 275-281 | 7 | |
| α-helix | 288-301 | 14 | |
| α-helix | 311-318 | 8 | |
| α-helix | 327-342 | 16 | |
| α-helix | 344-347 | 4 | |
| α-helix | 352-368 | 17 | |
| α-helix | 374-380 | 7 | |
| α-helix | 388-399 | 12 | |
| α-helix | 401-403 | 3 | |
| α-helix | 408-412 | 5 | |
| α-helix | 416-418 | 3 | |
| α-helix | 421-423 | 3 | |
| α-helix | 425-426 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 2 | A, C | protein | 300 | HOMO SAPIENS | P24941 (AlphaFold model) |
| Cyclin-A2 | B, D | protein | 262 | HOMO SAPIENS | P20248 (AlphaFold model) |
>4BCK_1 CYCLIN-DEPENDENT KINASE 2 (chains A, C) GSMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKEL NHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFC HSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCK YYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKP SFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
>4BCK_2 CYCLIN-A2 (chains B, D) SVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNE TLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQ VLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKY LPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIR EKYKNSKYHGVSLLNPPETLNL
| ID | Name | Formula | Copies |
|---|---|---|---|
| SGM | Monothioglycerol | C3 H8 O2 S | 1 |
| T3E | 3-[[5-cyano-4-[4-methyl-2-(methylamino)-1,3-thiazol-5-yl]pyrimidin-2-yl]amino]b… | C16 H15 N7 O2 S2 | 2 |
Comparative Structural and Functional Studies of 4-(Thiazol- 5-Yl)-2-(Phenylamino)Pyrimidine-5-Carbonitrile Cdk9 Inhibitors Suggest the Basis for Isotype Selectivity. Hole, A.J., Baumli, S., Shao, H. et al. J Med Chem (2013) 56:660. DOI 10.1021/JM301495V · PubMed
Other PDB entries of the same protein (UniProt P24941 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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