Crystal structure of CDK4/cyclin D3. Determined by X-ray diffraction at 3.0 Å resolution. Released 10 Mar 2009.
Explore 3G33 in 3D Show helices and sheets RCSB PDB PDBe
3G33 contains 61 α-helices and 22 β-strands across 4 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 | 11 | 1 | |
| β-strand | 12-17 | 6 | 1 |
| β-strand | 25-29 | 5 | 1 |
| β-strand | 36-45 | 10 | 1 |
| β-strand | 49 | 1 | 2 |
| β-strand | 51 | 1 | 2 |
| α-helix | 56-71 | 16 | |
| β-strand | 76 | 1 | 3 |
| β-strand | 79-85 | 7 | 1 |
| β-strand | 91-99 | 9 | 1 |
| α-helix | 100 | 1 | |
| β-strand | 104 | 1 | 3 |
| α-helix | 105-110 | 6 | |
| α-helix | 119-138 | 20 | |
| β-strand | 151-153 | 3 | 3 |
| β-strand | 159-161 | 3 | 3 |
| α-helix | 177-180 | 4 | |
| α-helix | 188-192 | 5 | |
| α-helix | 200-211 | 12 | |
| α-helix | 224-235 | 12 | |
| α-helix | 237-239 | 3 | |
| α-helix | 251-253 | 3 | |
| α-helix | 259-261 | 3 | |
| α-helix | 262-265 | 4 | |
| α-helix | 271-280 | 10 | |
| α-helix | 291-295 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-34 | 11 | |
| α-helix | 35-38 | 4 | |
| α-helix | 54-70 | 17 | |
| α-helix | 77-91 | 15 | |
| α-helix | 96-98 | 3 | |
| α-helix | 99-114 | 16 | |
| α-helix | 118-120 | 3 | |
| α-helix | 123-127 | 5 | |
| α-helix | 134-147 | 14 | |
| α-helix | 157-160 | 4 | |
| α-helix | 161-166 | 6 | |
| α-helix | 175-191 | 17 | |
| α-helix | 193-195 | 3 | |
| α-helix | 200-213 | 14 | |
| α-helix | 222-233 | 12 | |
| α-helix | 237-252 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-17 | 6 | 4 |
| β-strand | 25-29 | 5 | 4 |
| β-strand | 36-45 | 10 | 4 |
| β-strand | 49 | 1 | 5 |
| β-strand | 51 | 1 | 5 |
| α-helix | 56-71 | 16 | |
| β-strand | 76 | 1 | 6 |
| β-strand | 79-85 | 7 | 4 |
| β-strand | 91-99 | 9 | 4 |
| α-helix | 100 | 1 | |
| β-strand | 104 | 1 | 6 |
| α-helix | 105-110 | 6 | |
| α-helix | 119-138 | 20 | |
| β-strand | 151-153 | 3 | 6 |
| β-strand | 159-161 | 3 | 6 |
| α-helix | 167-176 | 10 | |
| α-helix | 188-191 | 4 | |
| α-helix | 200-211 | 12 | |
| α-helix | 224-235 | 12 | |
| α-helix | 237-239 | 3 | |
| α-helix | 251-253 | 3 | |
| α-helix | 259-261 | 3 | |
| α-helix | 262-265 | 4 | |
| α-helix | 271-280 | 10 | |
| α-helix | 291-295 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-34 | 11 | |
| α-helix | 35-38 | 4 | |
| α-helix | 54-70 | 17 | |
| α-helix | 77-91 | 15 | |
| α-helix | 96-98 | 3 | |
| α-helix | 99-114 | 16 | |
| α-helix | 118-120 | 3 | |
| α-helix | 123-127 | 5 | |
| α-helix | 134-147 | 14 | |
| α-helix | 157-160 | 4 | |
| α-helix | 161-166 | 6 | |
| α-helix | 175-191 | 17 | |
| α-helix | 193-195 | 3 | |
| α-helix | 200-213 | 14 | |
| α-helix | 223-233 | 11 | |
| α-helix | 237-252 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division protein kinase 4 | A, C | protein | 308 | Homo sapiens | P11802 (AlphaFold model) |
| CCND3 protein | B, D | protein | 306 | Homo sapiens | P30281 (AlphaFold model) |
>3G33_1 Cell division protein kinase 4 (chains A, C) GPLGSMATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVR EVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAE TIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVV VTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPE DDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYL HKDEGNPE
>3G33_2 CCND3 protein (chains B, D) MDYKDDDDKSPGGSMELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQ CVQREIKPHMRKMLAYWMLEVCEEQRCEEEVFPLAMNYLDRYLSCVPTRKAQLQLLGAVC MLLASKLRETTPLTIEKLCIYTDHAVSPRQLRDWEVLVLGKLKWDLAAVIAHDFLAFILH RLSLPRDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVQGLGACSMSGDELT ELLAGITGTEVDCLRACQEQIEAALRESLREAAQTSSSPAPKAPRGSSSQGPSQTSTPTD VTAIHL
The structure of CDK4/cyclin D3 has implications for models of CDK activation. Takaki, T., Echalier, A., Brown, N.R. et al. Proc Natl Acad Sci U S A (2009) 106:4171-4176. DOI 10.1073/pnas.0809674106 · PubMed
Other PDB entries of the same protein (UniProt P11802 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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