Cryo-EM structure of CAK in complex with SY-5609. Determined by electron microscopy at 2.3 Å resolution. Released 25 Dec 2024.
Explore 8S0T in 3D Show helices and sheets RCSB PDB PDBe
8S0T contains 41 α-helices and 13 β-strands across 3 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 | 259-261 | 3 | |
| α-helix | 265-269 | 5 | |
| α-helix | 271-274 | 4 | |
| α-helix | 276-279 | 4 | |
| α-helix | 280-284 | 5 | |
| α-helix | 289-301 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 6-11 | 6 | |
| α-helix | 16-35 | 20 | |
| α-helix | 50-70 | 21 | |
| α-helix | 77-90 | 14 | |
| α-helix | 101-115 | 15 | |
| α-helix | 122-126 | 5 | |
| α-helix | 133-153 | 21 | |
| α-helix | 164-177 | 14 | |
| α-helix | 184-187 | 4 | |
| α-helix | 188-200 | 13 | |
| α-helix | 202-205 | 4 | |
| α-helix | 209-223 | 15 | |
| α-helix | 229-230 | 2 | |
| α-helix | 231-235 | 5 | |
| α-helix | 242-261 | 20 | |
| α-helix | 264-266 | 3 | |
| α-helix | 267-282 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-20 | 9 | 1 |
| β-strand | 24-31 | 8 | 1 |
| β-strand | 32 | 1 | 2 |
| β-strand | 34 | 1 | 2 |
| β-strand | 37-43 | 7 | 1 |
| α-helix | 57-66 | 10 | |
| β-strand | 74 | 1 | 3 |
| α-helix | 75-76 | 2 | |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 86-92 | 7 | 1 |
| β-strand | 96-97 | 2 | 3 |
| α-helix | 98-103 | 6 | |
| α-helix | 111-130 | 20 | |
| β-strand | 133-134 | 2 | 4 |
| α-helix | 140-142 | 3 | |
| β-strand | 143-145 | 3 | 3 |
| β-strand | 151-153 | 3 | 3 |
| β-strand | 160-161 | 2 | 4 |
| α-helix | 176-178 | 3 | |
| α-helix | 181-184 | 4 | |
| α-helix | 193-208 | 16 | |
| α-helix | 218-229 | 12 | |
| α-helix | 240-242 | 3 | |
| α-helix | 248-250 | 3 | |
| α-helix | 257-260 | 4 | |
| α-helix | 266-275 | 10 | |
| α-helix | 284-285 | 2 | |
| α-helix | 286-290 | 5 | |
| α-helix | 293-296 | 4 | |
| α-helix | 304-306 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CDK-activating kinase assembly factor MAT1 | H | protein | 93 | Homo sapiens | P51948 (AlphaFold model) |
| Cyclin-H | I | protein | 324 | Homo sapiens | P51946 (AlphaFold model) |
| Cyclin-dependent kinase 7 | J | protein | 349 | Homo sapiens | P50613 (AlphaFold model) |
>8S0T_1 CDK-activating kinase assembly factor MAT1 (chains H) SNAPVTFSTGIKMGQHISLAPIHKLEEALYEYQPLQIETYGPHVPELEMLGRLGYLNHVR AASPQDLAGGYTSSLACHRALQDAFSGLFWQPS
>8S0T_2 Cyclin-H (chains I) XMYHNSSQKRHWTFSSEEQLARLRADANRKFRCKAVANGKVLPNDPVFLEPHEEMTLCKY YEKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYHPRIIMLTCAFLACKVDEFN VSSPQFVGNLRESPLGQEKALEQILEYELLLIQQLNFHLIVHNPYRPFEGFLIDLKTRYP ILENPEILRKTADDFLNRIALTDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLK ENRTCLSQLLDIMKSMRNLVKKYEPPRSEEVAVLKQKLERCHSAELALNVITKKRKGYED DDYVSKKSKHEEEEWTDDDLVESL
>8S0T_3 Cyclin-dependent kinase 7 (chains J) SNAMALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINR TALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAY MLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRW YRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQW PDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSN RPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF
| ID | Name | Formula | Copies |
|---|---|---|---|
| YNK | 7-dimethylphosphoryl-3-[2-[[(3~{S})-6,6-dimethylpiperidin-3-yl]amino]-5-(triflu… | C23 H26 F3 N6 O P | 1 |
TFIIH kinase CDK7 drives cell proliferation through a common core transcription factor network. Jones, T., Feng, J., Luyties, O. et al. Sci Adv (2025) 11:eadr9660-eadr9660. DOI 10.1126/sciadv.adr9660 · PubMed
Other PDB entries of the same protein (UniProt P51948 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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