Crystal structure of human Cdk2-Spy1 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 5 Jul 2017.
Explore 5UQ2 in 3D Show helices and sheets RCSB PDB PDBe
5UQ2 contains 27 α-helices and 11 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 | 4-12 | 9 | 1 |
| β-strand | 16-23 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| α-helix | 46-55 | 10 | |
| β-strand | 63 | 1 | 2 |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 76-81 | 6 | 1 |
| β-strand | 85-86 | 2 | 2 |
| α-helix | 87-93 | 7 | |
| α-helix | 101-120 | 20 | |
| β-strand | 123-124 | 2 | 3 |
| α-helix | 130-132 | 3 | |
| β-strand | 133-135 | 3 | 2 |
| β-strand | 141-143 | 3 | 2 |
| β-strand | 150-151 | 2 | 3 |
| α-helix | 166-168 | 3 | |
| α-helix | 171-174 | 4 | |
| α-helix | 183-197 | 15 | |
| α-helix | 208-219 | 12 | |
| α-helix | 240-242 | 3 | |
| α-helix | 244-247 | 4 | |
| α-helix | 248-251 | 4 | |
| α-helix | 257-266 | 10 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-281 | 5 | |
| α-helix | 292-294 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 72-75 | 4 | |
| α-helix | 76-79 | 4 | |
| α-helix | 81-89 | 9 | |
| α-helix | 98-110 | 13 | |
| α-helix | 115-117 | 3 | |
| α-helix | 120-134 | 15 | |
| α-helix | 140-143 | 4 | |
| α-helix | 144-149 | 6 | |
| α-helix | 153-155 | 3 | |
| α-helix | 157-170 | 14 | |
| α-helix | 179-185 | 7 | |
| α-helix | 193-196 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 2 | A | protein | 301 | Homo sapiens | P24941 (AlphaFold model) |
| Speedy protein A | B | protein | 160 | Homo sapiens | Q5MJ70 (AlphaFold model) |
>5UQ2_1 Cyclin-dependent kinase 2 (chains A) GEFMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKE LNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAF CHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGC KYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYK PSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLR L
>5UQ2_2 Speedy protein A (chains B) GAMDPEFGPCLVIQRQDMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKF TISEHTRINFFIALYLANTVEEDEEETKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDY RAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRD
Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. McGrath, D.A., Fifield, B.A., Marceau, A.H. et al. EMBO J (2017) 36:2251-2262. DOI 10.15252/embj.201796905 · PubMed
Other PDB entries of the same protein (UniProt P24941 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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