Cryo-EM structure of CAK in complex with inhibitor CT7030. Determined by electron microscopy at 1.9 Å resolution. Released 20 Mar 2024.
Explore 8PLZ in 3D Show helices and sheets RCSB PDB PDBe
8PLZ contains 43 α-helices and 11 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 | 258-262 | 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 | 6-10 | 5 | |
| α-helix | 16-37 | 22 | |
| α-helix | 48-49 | 2 | |
| α-helix | 50-69 | 20 | |
| α-helix | 74-76 | 3 | |
| α-helix | 77-92 | 16 | |
| 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 | 203-205 | 3 | |
| α-helix | 209-223 | 15 | |
| α-helix | 229-230 | 2 | |
| α-helix | 231-235 | 5 | |
| α-helix | 238-240 | 3 | |
| α-helix | 242-260 | 19 | |
| α-helix | 264-266 | 3 | |
| α-helix | 267-282 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-21 | 8 | 1 |
| β-strand | 24-29 | 6 | 1 |
| β-strand | 38-41 | 4 | 1 |
| α-helix | 57-67 | 11 | |
| β-strand | 74 | 1 | 2 |
| α-helix | 75-76 | 2 | |
| β-strand | 77-81 | 5 | 1 |
| β-strand | 88-92 | 5 | 1 |
| β-strand | 96-97 | 2 | 2 |
| α-helix | 98-103 | 6 | |
| α-helix | 111-130 | 20 | |
| β-strand | 133-134 | 2 | 3 |
| α-helix | 140-142 | 3 | |
| β-strand | 143-145 | 3 | 2 |
| β-strand | 151-153 | 3 | 2 |
| β-strand | 160-161 | 2 | 3 |
| 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 | 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 | 300-303 | 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) |
>8PLZ_1 CDK-activating kinase assembly factor MAT1 (chains H) SNAPVTFSTGIKMGQHISLAPIHKLEEALYEYQPLQIETYGPHVPELEMLGRLGYLNHVR AASPQDLAGGYTSSLACHRALQDAFSGLFWQPS
>8PLZ_2 Cyclin-H (chains I) XMYHNSSQKRHWTFSSEEQLARLRADANRKFRCKAVANGKVLPNDPVFLEPHEEMTLCKY YEKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYHPRIIMLTCAFLACKVDEFN VSSPQFVGNLRESPLGQEKALEQILEYELLLIQQLNFHLIVHNPYRPFEGFLIDLKTRYP ILENPEILRKTADDFLNRIALTDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLK ENRTCLSQLLDIMKSMRNLVKKYEPPRSEEVAVLKQKLERCHSAELALNVITKKRKGYED DDYVSKKSKHEEEEWTDDDLVESL
>8PLZ_3 Cyclin-dependent kinase 7 (chains J) SNAMALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINR TALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAY MLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRW YRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQW PDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSN RPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZQ6 | (3~{R},4~{R})-4-[[[7-[(2-methoxyphenyl)methylamino]-3-propan-2-yl-pyrazolo[1,5-… | C23 H32 N6 O2 | 1 |
High-resolution cryo-EM of the human CDK-activating kinase for structure-based drug design. Cushing, V.I., Koh, A.F., Feng, J. et al. Nat Commun (2024) 15:2265-2265. DOI 10.1038/s41467-024-46375-9 · 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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