Structure of CDK9 in complex with cyclin T and a 2-amino-4-heteroaryl- pyrimidine inhibitor. Determined by X-ray diffraction at 3.08 Å resolution. Released 17 Apr 2013.
Explore 4BCG in 3D Show helices and sheets RCSB PDB PDBe
4BCG contains 32 α-helices and 13 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 | 15 | 1 | 1 |
| α-helix | 16-18 | 3 | |
| β-strand | 19-24 | 6 | 2 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-49 | 6 | 2 |
| α-helix | 61-72 | 12 | |
| β-strand | 78 | 1 | 3 |
| β-strand | 81-85 | 5 | 2 |
| β-strand | 86 | 1 | 1 |
| β-strand | 100-104 | 5 | 2 |
| β-strand | 108-109 | 2 | 3 |
| α-helix | 110-114 | 5 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 4 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 3 |
| β-strand | 163-165 | 3 | 3 |
| β-strand | 172-173 | 2 | 4 |
| α-helix | 192-194 | 3 | |
| α-helix | 197-200 | 4 | |
| α-helix | 209-224 | 16 | |
| α-helix | 234-245 | 12 | |
| α-helix | 256-258 | 3 | |
| α-helix | 262-265 | 4 | |
| α-helix | 275-283 | 9 | |
| α-helix | 286-295 | 10 | |
| α-helix | 304-305 | 2 | |
| α-helix | 306-311 | 6 | |
| α-helix | 313-315 | 3 | |
| α-helix | 320-321 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-20 | 5 | |
| α-helix | 23-26 | 4 | |
| α-helix | 31-51 | 21 | |
| α-helix | 56-69 | 14 | |
| α-helix | 80-94 | 15 | |
| α-helix | 101-112 | 12 | |
| α-helix | 124-143 | 20 | |
| α-helix | 153-163 | 11 | |
| α-helix | 168-184 | 17 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-208 | 16 | |
| α-helix | 212-214 | 3 | |
| α-helix | 221-225 | 5 | |
| α-helix | 231-247 | 17 | |
| α-helix | 251-255 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 9 | A | protein | 331 | HOMO SAPIENS | P50750 (AlphaFold model) |
| Cyclin-T1 | B | protein | 260 | HOMO SAPIENS | O60563 (AlphaFold model) |
>4BCG_1 CYCLIN-DEPENDENT KINASE 9 (chains A) GPAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGF PITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLV KFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKN SQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLA LISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLD PAQRIDSDDALNHDFFWSDPMPSDLKGMLST
>4BCG_2 CYCLIN-T1 (chains B) GPEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTI NTAIVYMHRFYMIQSFTRFPGNSVAPAALFLAAKVEGQPKKLEHVIKVAHTCLHPQESLP DTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMAT NSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTH ELLQILEKTPNRLKRIWNWR
| ID | Name | Formula | Copies |
|---|---|---|---|
| T3C | 2-[[3-(1,4-diazepan-1-yl)phenyl]amino]-4-[4-methyl-2-(methylamino)-1,3-thiazol-… | C21 H24 N8 S | 1 |
Water and common crystallization additives (GOL) are not listed.
Substituted 4-(Thiazol-5-Yl)-2-(Phenylamino)Pyrimidines are Highly Active Cdk9 Inhibitors: Synthesis, X-Ray Crystal Structure, Sar and Anti-Cancer Activities. Shao, H., Shi, S., Huang, S. et al. J Med Chem (2013) 56:640. DOI 10.1021/JM301475F · PubMed
Other PDB entries of the same protein (UniProt P50750 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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