Crystal structure of CDK4 in complex with CyclinD1 and P21. Determined by X-ray diffraction at 3.19 Å resolution. Released 25 Dec 2019.
Explore 6P8H in 3D Show helices and sheets RCSB PDB PDBe
6P8H contains 26 α-helices and 10 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 | 20-35 | 16 | |
| α-helix | 54-70 | 17 | |
| α-helix | 77-89 | 13 | |
| α-helix | 99-114 | 16 | |
| α-helix | 121-127 | 7 | |
| α-helix | 134-147 | 14 | |
| α-helix | 157-167 | 11 | |
| α-helix | 172-191 | 20 | |
| α-helix | 194-197 | 4 | |
| α-helix | 200-212 | 13 | |
| α-helix | 226-236 | 11 | |
| α-helix | 241-260 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20-22 | 3 | 1 |
| β-strand | 32-39 | 8 | 1 |
| β-strand | 42 | 1 | 2 |
| β-strand | 45 | 1 | 2 |
| α-helix | 48-60 | 13 | |
| β-strand | 68 | 1 | 3 |
| β-strand | 71-77 | 7 | 1 |
| β-strand | 84-91 | 8 | 1 |
| β-strand | 96 | 1 | 3 |
| α-helix | 97-102 | 6 | |
| α-helix | 111-130 | 20 | |
| α-helix | 140-142 | 3 | |
| β-strand | 143-145 | 3 | 3 |
| β-strand | 151-153 | 3 | 3 |
| α-helix | 180-183 | 4 | |
| α-helix | 192-206 | 15 | |
| α-helix | 216-227 | 12 | |
| α-helix | 236 | 1 | |
| α-helix | 243-245 | 3 | |
| α-helix | 254-256 | 3 | |
| α-helix | 263-272 | 10 | |
| α-helix | 281-282 | 2 | |
| α-helix | 283-288 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-46 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| G1/S-specific cyclin-D1 | A | protein | 249 | Homo sapiens | P24385 (AlphaFold model) |
| Cyclin-dependent kinase 4 | B | protein | 302 | Homo sapiens | P11802 (AlphaFold model) |
| Cyclin-dependent kinase inhibitor 1 | C | protein | 80 | Homo sapiens | P38936 (AlphaFold model) |
>6P8H_1 G1/S-specific cyclin-D1 (chains A) DANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVF PLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELL QMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISN PPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESS LRQAQQNMD
>6P8H_2 Cyclin-dependent kinase 4 (chains B) GEFATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGEEGLPISTVREVALLR RLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLM RQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYR APEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRD VSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGN PE
>6P8H_3 Cyclin-dependent kinase inhibitor 1 (chains C) GEFRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAW ERVRGLGLPKLYLPTGPRRG
p27 allosterically activates cyclin-dependent kinase 4 and antagonizes palbociclib inhibition. Guiley, K.Z., Stevenson, J.W., Lou, K. et al. Science (2019) 366. DOI 10.1126/science.aaw2106 · PubMed
Other PDB entries of the same protein (UniProt P24385 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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