4YC6: CDK1/CKS1
CDK1/CKS1. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 May 2015.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 12,339
- Mol. weight
- 178.6 kDa
- Released
- 20 May 2015
Explore 4YC6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4YC6 contains 84 α-helices and 64 β-strands across 8 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.
Chains A, C and E: 17 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 1 |
| β-strand | 17-23 | 7 | 1 |
| β-strand | 29-36 | 8 | 1 |
| α-helix | 37-39 | 3 | |
| β-strand | 40-41 | 2 | 2 |
| α-helix | 47-56 | 10 | |
| β-strand | 63 | 1 | 3 |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 85-86 | 2 | 3 |
| α-helix | 87-92 | 6 | |
| α-helix | 95 | 1 | |
| α-helix | 102-121 | 20 | |
| α-helix | 131-133 | 3 | |
| β-strand | 134-136 | 3 | 3 |
| β-strand | 142-144 | 3 | 3 |
| α-helix | 149-152 | 4 | |
| α-helix | 166-169 | 4 | |
| α-helix | 172-175 | 4 | |
| β-strand | 180-181 | 2 | 4 |
| α-helix | 184-199 | 16 | |
| α-helix | 209-220 | 12 | |
| α-helix | 231-233 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 250-252 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-281 | 4 | |
Chain B: 4 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 5 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-13 | 2 | 5 |
| β-strand | 17-23 | 7 | 5 |
| α-helix | 26-31 | 6 | |
| α-helix | 37-39 | 3 | |
| α-helix | 40-44 | 5 | |
| β-strand | 55-58 | 4 | 5 |
| β-strand | 66-72 | 7 | 5 |
Chain D: 3 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 10 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-13 | 2 | 10 |
| β-strand | 17-23 | 7 | 10 |
| α-helix | 26-31 | 6 | |
| α-helix | 40-46 | 7 | |
| β-strand | 55-58 | 4 | 10 |
| β-strand | 66-72 | 7 | 10 |
Chain F: 4 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 13 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-13 | 2 | 13 |
| β-strand | 17-23 | 7 | 13 |
| α-helix | 26-31 | 6 | |
| α-helix | 37-39 | 3 | |
| α-helix | 40-45 | 6 | |
| β-strand | 55-58 | 4 | 13 |
| β-strand | 66-72 | 7 | 13 |
Chain G: 17 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-9 | 6 | 14 |
| β-strand | 17-23 | 7 | 14 |
| β-strand | 29-36 | 8 | 14 |
| α-helix | 37-38 | 2 | |
| β-strand | 40-41 | 2 | 4 |
| α-helix | 47-56 | 10 | |
| β-strand | 63 | 1 | 15 |
| β-strand | 66-71 | 6 | 14 |
| β-strand | 75-81 | 7 | 14 |
| β-strand | 85-86 | 2 | 15 |
| α-helix | 87-92 | 6 | |
| α-helix | 95 | 1 | |
| α-helix | 102-121 | 20 | |
| α-helix | 131-133 | 3 | |
| β-strand | 134-136 | 3 | 15 |
| β-strand | 142-144 | 3 | 15 |
| α-helix | 149-152 | 4 | |
| α-helix | 166-169 | 4 | |
| α-helix | 172-175 | 4 | |
| β-strand | 180-181 | 2 | 2 |
| α-helix | 184-199 | 16 | |
| α-helix | 209-220 | 12 | |
| α-helix | 231-233 | 3 | |
| α-helix | 244-246 | 3 | |
| α-helix | 250-252 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-281 | 4 | |
Chain H: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 16 |
| α-helix | 9-11 | 3 | |
| β-strand | 12-13 | 2 | 16 |
| β-strand | 17-23 | 7 | 16 |
| α-helix | 24-25 | 2 | |
| α-helix | 26-31 | 6 | |
| α-helix | 37-39 | 3 | |
| α-helix | 40-45 | 6 | |
| β-strand | 55-58 | 4 | 16 |
| β-strand | 66-72 | 7 | 16 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cyclin-dependent kinase 1 | A, C, E, G | protein | 297 | Homo sapiens | P06493 (AlphaFold model) |
| Cyclin-dependent kinases regulatory subunit 1 | B, D, F, H | protein | 85 | Homo sapiens | P61024 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>4YC6_1 Cyclin-dependent kinase 1 (chains A, C, E, G)
MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRH
PNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCH
SRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSAR
YSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNT
FPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM
Sequence of entity 2 (B, D, F, H), FASTA
>4YC6_2 Cyclin-dependent kinases regulatory subunit 1 (chains B, D, F, H)
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIH
EPEPHILLFRRPLPKKPKKHHHHHH
Primary citation
CDK1 structures reveal conserved and unique features of the essential cell cycle CDK. Brown, N.R., Korolchuk, S., Martin, M.P. et al. Nat Commun (2015) 6:6769-6769. DOI 10.1038/ncomms7769 · PubMed
Other PDB entries of the same protein (UniProt P06493 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6GU2 2.0 Å, CDK1/CyclinB/Cks2 in complex with Flavopiridol
- 5LQF 2.06 Å, CDK1/CyclinB1/CKS2 in complex with NU6102
- 6TWN 2.28 Å, Crystal structure of Talin1 R7R8 in complex with CDK1 (206-223)
- 4Y72 2.3 Å, Human CDK1/CyclinB1/CKS2 With Inhibitor
- 5HQ0 2.3 Å, Ternary complex of human proteins CDK1, Cyclin B and CKS2, bound to an inhibitor
- 6GU6 2.33 Å, CDK1/Cks2 in complex with Dinaciclib
- 11GY 2.4 Å, Crystal structure of selective inhibitor 16 bound at the active site of CDK1
- 6GU3 2.65 Å, CDK1/CyclinB/Cks2 in complex with AZD5438
- 4YC3 2.7 Å, CDK1/CyclinB1/CKS2 Apo
- 6GU4 2.73 Å, CDK1/CyclinB/Cks2 in complex with CGP74514A
- 6GU7 2.75 Å, CDK1/Cks2 in complex with AZD5438
- 9SKQ 3.4 Å, Cryo-EM structure of CAK-CDK1-cyclin B1
Browse structure collections
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