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- PDB-9hiu: Cryo-EM structure of CDK2-cyclin A bound to a GMNC peptide -

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Basic information

Entry
Database: PDB / ID: 9hiu
TitleCryo-EM structure of CDK2-cyclin A bound to a GMNC peptide
Components
  • Cyclin-A2
  • Cyclin-dependent kinase 2
  • Geminin coiled-coil domain-containing protein 1
KeywordsCELL CYCLE / Kinase / cyclin / short linear motif / cdk2 / cyclin A
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)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å
Authorsde Martin Garrido, N. / Ord, M. / Cushing, V.I. / Greber, B.J. / Pryciak, P.M. / Davey, N.E.
Funding support1items
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, M.J. / Subbanna, M. / de Martin Garrido, N. / Cushing, V.I. / Kliche, J. / Benz, C. / Ivarsson, Y. / Greber, B.J. / Pryciak, P.M. / Davey, N.E.
History
DepositionNov 27, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 20, 2025Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Aug 20, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cyclin-A2
B: Cyclin-dependent kinase 2
C: Geminin coiled-coil domain-containing protein 1


Theoretical massNumber of molelcules
Total (without water)83,9413
Polymers83,9413
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Cyclin-A2 / Cyclin-A / Cyclin A


Mass: 48595.547 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CCNA2, CCN1, CCNA / Production host: Escherichia coli (E. coli) / References: UniProt: P20248
#2: Protein Cyclin-dependent kinase 2 / Cell division protein kinase 2 / p33 protein kinase


Mass: 33863.332 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDK2, CDKN2 / Production host: Escherichia coli (E. coli) / References: UniProt: P24941, cyclin-dependent kinase
#3: Protein/peptide Geminin coiled-coil domain-containing protein 1


Mass: 1481.634 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: A6NCL1
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: CDK2-cyclin A bound to a GMNC peptide / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli) / Strain: Rosetta (DE3) pLysS
Buffer solutionpH: 7.5
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMHEPESHEPES-NaOH1
2150 mMsodium chlorideNaCl1
32 mMmagnesium chlorideMgCl21
SpecimenConc.: 0.4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 278.15 K

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Electron microscopy imaging

MicroscopyModel: TFS GLACIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Calibrated magnification: 246696 X / Nominal defocus max: 1800 nm / Nominal defocus min: 600 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 60 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 6422

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Processing

EM software
IDNameVersionCategory
1cryoSPARCv4.4.1particle selection
2EPUimage acquisition
4cryoSPARCv4.4.1CTF correction
5RELION5.0 betaCTF correction
8UCSF ChimeraXmodel fitting
10RELION5.0 betainitial Euler assignment
11RELION5.0 betafinal Euler assignment
13RELION5.0 beta3D reconstruction
14PHENIX1.21.1_5286model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 183712 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
Atomic model buildingSource name: AlphaFold / Type: in silico model
RefinementHighest resolution: 3.2 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0024547
ELECTRON MICROSCOPYf_angle_d0.4356163
ELECTRON MICROSCOPYf_dihedral_angle_d3.528595
ELECTRON MICROSCOPYf_chiral_restr0.037697
ELECTRON MICROSCOPYf_plane_restr0.004775

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