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- EMDB-52201: Cryo-EM structure of CDK2-cyclin A bound to a GMNC peptide -

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Basic information

Entry
Database: EMDB / ID: EMD-52201
TitleCryo-EM structure of CDK2-cyclin A bound to a GMNC peptide
Map dataPost-processed cryo-EM map
Sample
  • Complex: CDK2-cyclin A bound to a GMNC peptide
    • Protein or peptide: Cyclin-A2
    • Protein or peptide: Cyclin-dependent kinase 2
    • Protein or peptide: Geminin coiled-coil domain-containing protein 1
KeywordsKinase / cyclin / short linear motif / cdk2 / cyclin A / CELL CYCLE
Function / homology
Function and homology information


multi-ciliated epithelial cell differentiation / cerebrospinal fluid circulation / : / cyclin A2-CDK1 complex / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / seminiferous tubule development / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / cellular response to leptin stimulus / male pronucleus ...multi-ciliated epithelial cell differentiation / cerebrospinal fluid circulation / : / cyclin A2-CDK1 complex / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / seminiferous tubule development / 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 / regulation of DNA-templated DNA replication initiation / cyclin-dependent protein serine/threonine kinase regulator activity / positive regulation of DNA biosynthetic process / cellular response to insulin-like growth factor stimulus / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex / cyclin E1-CDK2 complex / cyclin A2-CDK2 complex / positive regulation of DNA-templated DNA replication initiation / cyclin-dependent protein kinase activity / G2 Phase / Y chromosome / 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) / microtubule organizing center / centriole replication / Regulation of APC/C activators between G1/S and early anaphase / negative regulation of cell cycle / telomere maintenance in response to DNA damage / regulation of DNA replication / centrosome duplication / G0 and Early G1 / cochlea development / Telomere Extension By Telomerase / cilium assembly / animal organ regeneration / Activation of the pre-replicative complex / cyclin-dependent kinase / single fertilization / cyclin-dependent protein serine/threonine kinase activity / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / Cajal body / Activation of ATR in response to replication stress / Cyclin E associated events during G1/S transition / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / cyclin-dependent protein kinase holoenzyme complex / condensed chromosome / cellular response to platelet-derived growth factor stimulus / regulation of G2/M transition of mitotic cell cycle / mitotic G1 DNA damage checkpoint signaling / cellular response to nitric oxide / post-translational protein modification / cyclin binding / regulation of mitotic cell cycle / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / positive regulation of DNA replication / meiotic cell cycle / male germ cell nucleus / cellular response to estradiol stimulus / CDK-mediated phosphorylation and removal of Cdc6 / G1/S transition of mitotic cell cycle / SCF(Skp2)-mediated degradation of p27/p21 / peptidyl-serine phosphorylation / DNA Damage/Telomere Stress Induced Senescence / Orc1 removal from chromatin / potassium ion transport / Meiotic recombination / Cyclin D associated events in G1 / G2/M transition of mitotic cell cycle / multicellular organism growth / Transcriptional regulation of granulopoiesis / positive regulation of fibroblast proliferation / Regulation of TP53 Degradation / cellular senescence / nuclear envelope / Processing of DNA double-strand break ends / regulation of gene expression / Senescence-Associated Secretory Phenotype (SASP) / Factors involved in megakaryocyte development and platelet production / Regulation of TP53 Activity through Phosphorylation / spermatogenesis / cellular response to hypoxia / transcription regulator complex / Ras protein signal transduction / chromosome, telomeric region / DNA replication / protein phosphorylation / Ub-specific processing proteases / endosome / chromatin remodeling
Similarity search - Function
Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin, C-terminal domain / Cyclin_C / Cyclin, N-terminal ...Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin, C-terminal domain / Cyclin_C / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like 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
Geminin coiled-coil domain-containing protein 1 / Cyclin-A2 / Cyclin-dependent kinase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
Authorsde Martin Garrido N / Ord M / Cushing VI / Greber BJ / Pryciak PM / Davey NE
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Cryo-EM structure of CDK2-cyclin A bound to a GMNC peptide
Authors: Ord M / Winters MJ / Subbanna M / de Martin Garrido N / Cushing VI / Kliche J / Benz C / Ivarsson Y / Greber BJ / Pryciak PM / Davey NE
History
DepositionNov 27, 2024-
Header (metadata) releaseAug 20, 2025-
Map releaseAug 20, 2025-
UpdateAug 20, 2025-
Current statusAug 20, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52201.png

Downloads & links

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Map

FileDownload / File: emd_52201.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPost-processed cryo-EM map
Projections & slices

Image control

Size
Brightness
Contrast
Others
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

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.135 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.024
Minimum - Maximum-0.08802457 - 0.14592606
Average (Standard dev.)-0.0000064736173 (±0.005466288)
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_52201_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unfiltered half-map (RELION Refine3D)

Fileemd_52201_half_map_1.map
AnnotationUnfiltered half-map (RELION Refine3D)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unfiltered half-map (RELION Refine3D)

Fileemd_52201_half_map_2.map
AnnotationUnfiltered half-map (RELION Refine3D)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : CDK2-cyclin A bound to a GMNC peptide

EntireName: CDK2-cyclin A bound to a GMNC peptide
Components
  • Complex: CDK2-cyclin A bound to a GMNC peptide
    • Protein or peptide: Cyclin-A2
    • Protein or peptide: Cyclin-dependent kinase 2
    • Protein or peptide: Geminin coiled-coil domain-containing protein 1

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

SupramoleculeName: CDK2-cyclin A bound to a GMNC 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: Geminin coiled-coil domain-containing protein 1

MacromoleculeName: Geminin coiled-coil domain-containing protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.481634 KDa
SequenceString:
KNAKRNLSSE FAN

UniProtKB: Geminin coiled-coil domain-containing protein 1

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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 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 50 sec.
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: 6422 / 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 reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.0 beta) / Number images used: 183712
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: 500000
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-9hiu:
Cryo-EM structure of CDK2-cyclin A bound to a GMNC peptide

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