Crystal structure of phospho-CDK2 in complex with Cyclin B. Determined by X-ray diffraction at 2.9 Å resolution. Released 22 May 2007.
Explore 2JGZ in 3D Show helices and sheets RCSB PDB PDBe
2JGZ contains 33 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 | 17-23 | 7 | 1 |
| β-strand | 29-36 | 8 | 1 |
| α-helix | 46-57 | 12 | |
| β-strand | 63 | 1 | 2 |
| α-helix | 64-65 | 2 | |
| β-strand | 66-73 | 8 | 1 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 85-86 | 2 | 2 |
| α-helix | 87-93 | 7 | |
| α-helix | 101-119 | 19 | |
| 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 | 183-198 | 16 | |
| α-helix | 208-219 | 12 | |
| α-helix | 230-232 | 3 | |
| α-helix | 243-247 | 5 | |
| α-helix | 248-251 | 4 | |
| α-helix | 257-265 | 9 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-280 | 4 | |
| α-helix | 284-286 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 171-184 | 14 | |
| α-helix | 199-216 | 18 | |
| α-helix | 220-234 | 15 | |
| α-helix | 241-243 | 3 | |
| α-helix | 244-259 | 16 | |
| α-helix | 263-265 | 3 | |
| α-helix | 266-272 | 7 | |
| α-helix | 279-293 | 15 | |
| α-helix | 302-311 | 10 | |
| α-helix | 317-330 | 14 | |
| α-helix | 334-336 | 3 | |
| α-helix | 341-355 | 15 | |
| α-helix | 363-368 | 6 | |
| α-helix | 373-391 | 19 | |
| α-helix | 399-403 | 5 | |
| α-helix | 407-409 | 3 | |
| α-helix | 412-414 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division protein kinase 2 | A | protein | 289 | HOMO SAPIENS | P24941 (AlphaFold model) |
| G2/MITOTIC-specific cyclin-B1 | B | protein | 260 | HOMO SAPIENS | P14635 (AlphaFold model) |
>2JGZ_1 CELL DIVISION PROTEIN KINASE 2 (chains A) SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELN HPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKY YSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQD
>2JGZ_2 G2/MITOTIC-SPECIFIC CYCLIN-B1 (chains B) CSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMT VSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQME MKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAA GAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYAT SKHAKISTLPQLNSALVQDL
Cyclin B and cyclin A confer different substrate recognition properties on CDK2. Brown, N.R., Lowe, E.D., Petri, E. et al. Cell Cycle (2007) 6:1350-1359. DOI 10.4161/cc.6.11.4278 · 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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