CDK1/CyclinB/Cks2 in complex with CGP74514A. Determined by X-ray diffraction at 2.73 Å resolution. Released 5 Dec 2018.
Explore 6GU4 in 3D Show helices and sheets RCSB PDB PDBe
6GU4 contains 39 α-helices and 17 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 | 1-3 | 3 | |
| β-strand | 4-12 | 9 | 1 |
| β-strand | 17-23 | 7 | 1 |
| β-strand | 28-35 | 8 | 1 |
| α-helix | 36 | 1 | |
| α-helix | 46-56 | 11 | |
| 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 | 99-101 | 3 | |
| α-helix | 102-120 | 19 | |
| β-strand | 124-125 | 2 | 3 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-136 | 3 | 2 |
| β-strand | 142-144 | 3 | 2 |
| β-strand | 151-152 | 2 | 3 |
| β-strand | 155-156 | 2 | 3 |
| α-helix | 172-175 | 4 | |
| α-helix | 184-199 | 16 | |
| α-helix | 209-220 | 12 | |
| α-helix | 231-233 | 3 | |
| α-helix | 250-252 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-282 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 170-183 | 14 | |
| α-helix | 198-214 | 17 | |
| α-helix | 219-235 | 17 | |
| α-helix | 240-242 | 3 | |
| α-helix | 243-258 | 16 | |
| α-helix | 262-264 | 3 | |
| α-helix | 265-271 | 7 | |
| α-helix | 278-291 | 14 | |
| α-helix | 301-311 | 11 | |
| α-helix | 316-329 | 14 | |
| α-helix | 333-335 | 3 | |
| α-helix | 340-354 | 15 | |
| α-helix | 362-368 | 7 | |
| α-helix | 372-390 | 19 | |
| α-helix | 398-402 | 5 | |
| α-helix | 406-408 | 3 | |
| α-helix | 411-413 | 3 | |
| α-helix | 415-418 | 4 | |
| α-helix | 420-427 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-8 | 2 | 4 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-13 | 2 | 4 |
| β-strand | 17-23 | 7 | 4 |
| α-helix | 24-25 | 2 | |
| α-helix | 26-29 | 4 | |
| α-helix | 37-39 | 3 | |
| α-helix | 40-46 | 7 | |
| β-strand | 55-60 | 6 | 4 |
| β-strand | 63-72 | 10 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 1 | A | protein | 302 | Homo sapiens | P06493 (AlphaFold model) |
| G2/mitotic-specific cyclin-B1 | B | protein | 273 | Homo sapiens | P14635 (AlphaFold model) |
| Cyclin-dependent kinases regulatory subunit 2 | C | protein | 84 | Homo sapiens | P33552 (AlphaFold model) |
>6GU4_1 Cyclin-dependent kinase 1 (chains A) GPLGSMEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLL KELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQG IVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVL LGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQ DYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIK KM
>6GU4_2 G2/mitotic-specific cyclin-B1 (chains B) GSHMNLSSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQ ETMYMTVSIIDRFMQNNSVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKH QIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFP PSQIAAGAFSLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTV KNKYATSKHAKISTLPQLNSALVQDLAKAVAKV
>6GU4_3 Cyclin-dependent kinases regulatory subunit 2 (chains C) GPLGSMAHKQIYYSDKYFDEHYEYRHVMLPRELSKQVPKTHLMSEEEWRRLGVQQSLGWV HYMIHEPEPHILLFRRPLPKDQQK
| ID | Name | Formula | Copies |
|---|---|---|---|
| FC8 | ~{N}2-[(1~{R},2~{S})-2-azanylcyclohexyl]-~{N}6-(3-chlorophenyl)-9-ethyl-purine-… | C19 H24 Cl N7 | 1 |
Differences in the Conformational Energy Landscape of CDK1 and CDK2 Suggest a Mechanism for Achieving Selective CDK Inhibition. Wood, D.J., Korolchuk, S., Tatum, N.J. et al. Cell Chem Biol (2019) 26:121-130.e5. DOI 10.1016/j.chembiol.2018.10.015 · PubMed
Other PDB entries of the same protein (UniProt P06493 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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