Crystal structure of selective inhibitor 16 bound at the active site of CDK2. Determined by X-ray diffraction at 1.59 Å resolution. Released 2 Sept 2026.
Explore 11GV in 3D Show helices and sheets RCSB PDB PDBe
11GV contains 37 α-helices and 11 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 | 4-11 | 8 | 1 |
| β-strand | 17-23 | 7 | 1 |
| β-strand | 29-36 | 8 | 1 |
| α-helix | 46-55 | 10 | |
| β-strand | 63 | 1 | 2 |
| α-helix | 64-65 | 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 | 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 | 243-247 | 5 | |
| α-helix | 248-251 | 4 | |
| α-helix | 257-266 | 10 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-281 | 5 | |
| α-helix | 284-286 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 175-176 | 2 | |
| α-helix | 179-192 | 14 | |
| α-helix | 199-202 | 4 | |
| α-helix | 208-224 | 17 | |
| α-helix | 229-245 | 17 | |
| α-helix | 250-268 | 19 | |
| α-helix | 272-274 | 3 | |
| α-helix | 275-281 | 7 | |
| α-helix | 288-301 | 14 | |
| α-helix | 311-319 | 9 | |
| α-helix | 327-339 | 13 | |
| α-helix | 344-347 | 4 | |
| α-helix | 352-368 | 17 | |
| α-helix | 374-380 | 7 | |
| α-helix | 385-387 | 3 | |
| α-helix | 388-400 | 13 | |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 2 | A | protein | 298 | Homo sapiens | P24941 (AlphaFold model) |
| Cyclin-A2 | B | protein | 260 | Homo sapiens | P20248 (AlphaFold model) |
>11GV_1 Cyclin-dependent kinase 2 (chains A) MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
>11GV_2 Cyclin-A2 (chains B) MEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETL HLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLP SVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK YKNSKYHGVSLLNPPETLNL
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 3 |
| A1DEQ | (1R,3S)-3-{3-[(1-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)amino]-1H-pyrazol-5-yl}… | C19 H24 N6 O3 | 2 |
| IPA | Isopropyl alcohol | C3 H8 O | 1 |
Water and common crystallization additives (EDO, CL, DMS) are not listed.
Utilizing Molecular Dynamics and Mechanistic Pharmacokinetic Studies in the Design of Selective CDK2 Inhibitors. Verma, V.A., Grandner, J.M., Parr, B.T. et al. J Med Chem (2026) 69:15294-15316. DOI 10.1021/acs.jmedchem.5c03803 · 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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