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- EMDB-52204: Cryo-EM structure of CDK2-cyclin A bound to a SAMHD1 peptide -

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Entry
Database: EMDB / ID: EMD-52204
TitleCryo-EM structure of CDK2-cyclin A bound to a SAMHD1 peptide
Map data
Sample
  • Complex: CDK2-cyclin A bound to a SAMHD1 peptide
    • Protein or peptide: Cyclin-A2
    • Protein or peptide: Cyclin-dependent kinase 2
    • Protein or peptide: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
KeywordsKinase / cyclin / short linear motif / cdk2 / cyclin A / CELL CYCLE
Function / homology
Function and homology information


Nucleotide catabolism / Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases / deoxynucleoside triphosphate hydrolase activity / dGTP binding / dATP catabolic process / deoxyribonucleotide catabolic process / tetraspanin-enriched microdomain / dGTPase activity / cyclin A2-CDK1 complex / dGTP catabolic process ...Nucleotide catabolism / Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases / deoxynucleoside triphosphate hydrolase activity / dGTP binding / dATP catabolic process / deoxyribonucleotide catabolic process / tetraspanin-enriched microdomain / dGTPase activity / cyclin A2-CDK1 complex / dGTP catabolic process / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / DNA strand resection involved in replication fork processing / G2/M DNA replication checkpoint / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / cellular response to leptin stimulus / male pronucleus / female pronucleus / cellular response to cocaine / response to glucagon / cyclin-dependent protein serine/threonine kinase regulator activity / negative regulation of type I interferon-mediated signaling pathway / positive regulation of DNA biosynthetic process / cellular response to insulin-like growth factor stimulus / regulation of innate immune response / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex / regulation of heterochromatin organization / cyclin E1-CDK2 complex / cyclin A2-CDK2 complex / positive regulation of DNA-templated DNA replication initiation / G2 Phase / Y chromosome / cyclin-dependent protein kinase activity / Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes / positive regulation of heterochromatin formation / p53-Dependent G1 DNA Damage Response / X chromosome / PTK6 Regulates Cell Cycle / regulation of anaphase-promoting complex-dependent catabolic process / Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) / centriole replication / Regulation of APC/C activators between G1/S and early anaphase / telomere maintenance in response to DNA damage / regulation of DNA replication / centrosome duplication / microtubule organizing center / G0 and Early G1 / cochlea development / animal organ regeneration / Telomere Extension By Telomerase / Activation of the pre-replicative complex / RNA nuclease activity / cyclin-dependent kinase / cyclin-dependent protein serine/threonine kinase activity / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Activation of ATR in response to replication stress / Cyclin E associated events during G1/S transition / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / Cajal body / somatic hypermutation of immunoglobulin genes / Cyclin A:Cdk2-associated events at S phase entry / Cyclin A/B1/B2 associated events during G2/M transition / cyclin-dependent protein kinase holoenzyme complex / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / regulation of G2/M transition of mitotic cell cycle / negative regulation of protein localization to chromatin / cellular response to platelet-derived growth factor stimulus / condensed chromosome / mitotic G1 DNA damage checkpoint signaling / cellular response to nitric oxide / post-translational protein modification / regulation of mitotic cell cycle / cyclin binding / positive regulation of DNA replication / male germ cell nucleus / meiotic cell cycle / potassium ion transport / cellular response to estradiol stimulus / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / peptidyl-serine phosphorylation / G1/S transition of mitotic cell cycle / double-strand break repair via homologous recombination / DNA Damage/Telomere Stress Induced Senescence / CDK-mediated phosphorylation and removal of Cdc6 / Meiotic recombination / G2/M transition of mitotic cell cycle / SCF(Skp2)-mediated degradation of p27/p21 / positive regulation of fibroblast proliferation / Transcriptional regulation of granulopoiesis / Orc1 removal from chromatin / Cyclin D associated events in G1 / Interferon alpha/beta signaling / cellular senescence / Regulation of TP53 Degradation / nuclear envelope / single-stranded DNA binding / site of double-strand break / Factors involved in megakaryocyte development and platelet production / regulation of gene expression
Similarity search - Function
: / Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / HD domain profile. / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / HD domain ...: / Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / HD domain profile. / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / HD domain / Cyclin, C-terminal domain / Cyclin_C / HD domain / Cyclin, N-terminal / Cyclin, N-terminal domain / SAM domain (Sterile alpha motif) / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / SAM domain profile. / Metal dependent phosphohydrolases with conserved 'HD' motif. / : / HD/PDEase domain / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Cyclin-A2 / Cyclin-dependent kinase 2 / Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
Authorsde Martin Garrido N / Ord M / Cushing VI / Greber BJ / Pryciak PM / Davey NE
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Commun / Year: 2025
Title: High-throughput investigation of cyclin docking interactions reveals the complexity of motif binding determinants.
Authors: Mihkel Örd / Matthew J Winters / Mythili S Subbanna / Natàlia de Martín Garrido / Victoria I Cushing / Johanna Kliche / Caroline Benz / Ylva Ivarsson / Basil J Greber / Peter M Pryciak / Norman E Davey /
Abstract: Many regulatory protein-protein interactions depend on Short Linear Motifs (SLiMs). In the cell cycle, cyclin-CDKs recognize SLiMs to control substrate recruitment and phosphorylation timing. Here, ...Many regulatory protein-protein interactions depend on Short Linear Motifs (SLiMs). In the cell cycle, cyclin-CDKs recognize SLiMs to control substrate recruitment and phosphorylation timing. Here, we measure the relative binding strength of ~100,000 peptides to 11 human cyclins from five families (D, E, A, B, and F). Using a quantitative intracellular binding assay and large-scale tiled peptide screening, we identify multiple non-canonical binders unveiling a broader repertoire of cyclin docking motif types. Cryo-electron microscopy and saturation mutagenesis studies reveal distinct binding modes and sequence features governing motif recognition, binding strength, and cyclin preference. Docking motifs vary from highly selective to pan-cyclin, thereby fine-tuning the timing of CDK phosphorylation during cell cycle. Overall, these findings provide insights into the rules encoding specificity and affinity of SLiM-mediated interactions and offer a framework for understanding motif-driven protein networks across the proteome.
History
DepositionNov 27, 2024-
Header (metadata) releaseAug 20, 2025-
Map releaseAug 20, 2025-
UpdateMar 4, 2026-
Current statusMar 4, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52204.png

Downloads & links

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Map

FileDownload / File: emd_52204.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.14 Å/pix.
x 160 pix.
= 181.6 Å		1.14 Å/pix.
x 160 pix.
= 181.6 Å		1.14 Å/pix.
x 160 pix.
= 181.6 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.135 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.024
Minimum - Maximum-0.09263781 - 0.14258191
Average (Standard dev.)0.0000009897525 (±0.0052111135)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions160160160
Spacing160160160
CellA=B=C: 181.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_52204_msk_1.map
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Half map: #2

Fileemd_52204_half_map_1.map
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Half map: #1

Fileemd_52204_half_map_2.map
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Sample components

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Entire : CDK2-cyclin A bound to a SAMHD1 peptide

EntireName: CDK2-cyclin A bound to a SAMHD1 peptide
Components
  • Complex: CDK2-cyclin A bound to a SAMHD1 peptide
    • Protein or peptide: Cyclin-A2
    • Protein or peptide: Cyclin-dependent kinase 2
    • Protein or peptide: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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Supramolecule #1: CDK2-cyclin A bound to a SAMHD1 peptide

SupramoleculeName: CDK2-cyclin A bound to a SAMHD1 peptide / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Cyclin-A2

MacromoleculeName: Cyclin-A2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 48.595547 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL AVLKSGNPRG LAQQQRPKTR RVAPLKDLPV NDEHVTVPP WKANSKQPAF TIHVDEAEKE AQKKPAESQK IEREDALAFN SAISLPGPRK PLVPLDYPMD GSFESPHTMD M SIVLEDEK ...String:
MLGNSAPGPA TREAGSALLA LQQTALQEDQ ENINPEKAAP VQQPRTRAAL AVLKSGNPRG LAQQQRPKTR RVAPLKDLPV NDEHVTVPP WKANSKQPAF TIHVDEAEKE AQKKPAESQK IEREDALAFN SAISLPGPRK PLVPLDYPMD GSFESPHTMD M SIVLEDEK PVSVNEVPDY HEDIHTYLRE MEVKCKPKVG YMKKQPDITN SMRAILVDWL VEVGEEYKLQ NETLHLAVNY ID RFLSSMS VLRGKLQLVG TAAMLLASKF EEIYPPEVAE FVYITDDTYT KKQVLRMEHL VLKVLTFDLA APTVNQFLTQ YFL HQQPAN CKVESLAMFL GELSLIDADP YLKYLPSVIA GAAFHLALYT VTGQSWPESL IRKTGYTLES LKPCLMDLHQ TYLK APQHA QQSIREKYKN SKYHGVSLLN PPETLNL

UniProtKB: Cyclin-A2

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Macromolecule #2: Cyclin-dependent kinase 2

MacromoleculeName: Cyclin-dependent kinase 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: cyclin-dependent kinase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 33.863332 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH PNIVKLLDVI HTENKLYLVF EFLHQDLKK FMDASALTGI PLPLIKSYLF QLLQGLAFCH SHRVLHRDLK PQNLLINTEG AIKLADFGLA RAFGVPVRTY T HEVVTLWY ...String:
MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH PNIVKLLDVI HTENKLYLVF EFLHQDLKK FMDASALTGI PLPLIKSYLF QLLQGLAFCH SHRVLHRDLK PQNLLINTEG AIKLADFGLA RAFGVPVRTY T HEVVTLWY RAPEILLGCK YYSTAVDIWS LGCIFAEMVT RRALFPGDSE IDQLFRIFRT LGTPDEVVWP GVTSMPDYKP SF PKWARQD FSKVVPPLDE DGRSLLSQML HYDPNKRISA KAALAHPFFQ DVTKPVPHLR

UniProtKB: Cyclin-dependent kinase 2

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Macromolecule #3: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

MacromoleculeName: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.553802 KDa
SequenceString:
SKSRVQLFKD DPM

UniProtKB: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.4 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
20.0 mMHEPES-NaOHHEPES
150.0 mMNaClsodium chloride
2.0 mMMgCl2magnesium chloride
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 278.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Number grids imaged: 1 / Number real images: 5078 / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated magnification: 246696 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.6 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN

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Image processing

CTF correctionSoftware: (Name: cryoSPARC (ver. v4.4.1), RELION (ver. 5.0 beta))
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: Alphafold model of CDK2-cyclin A
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.0 beta) / Number images used: 80673
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 5.0 beta)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 5.0 beta)
Final 3D classificationNumber classes: 4 / Avg.num./class: 360000
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9hiw:
Cryo-EM structure of CDK2-cyclin A bound to a SAMHD1 peptide

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