+Open data
-Basic information
Entry | Database: PDB / ID: 1fin | ||||||
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Title | CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX | ||||||
Components |
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Keywords | COMPLEX (TRANSFERASE/CYCLIN) / COMPLEX (TRANSFERASE-CYCLIN) / CYCLIN / CDK / PHOSPHORYLATION / COMPLEX (TRANSFERASE-CYCLIN) complex | ||||||
Function / homology | Function and homology information G2 Phase / Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes / cyclin A2-CDK1 complex / cyclin A2-CDK2 complex / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / p53-Dependent G1 DNA Damage Response / mitotic cell cycle phase transition / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / Regulation of APC/C activators between G1/S and early anaphase ...G2 Phase / Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes / cyclin A2-CDK1 complex / cyclin A2-CDK2 complex / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / p53-Dependent G1 DNA Damage Response / mitotic cell cycle phase transition / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / Regulation of APC/C activators between G1/S and early anaphase / cellular response to leptin stimulus / male pronucleus / Telomere Extension By Telomerase / G0 and Early G1 / female pronucleus / response to glucagon / cellular response to cocaine / cellular response to nitric oxide / cyclin-dependent protein serine/threonine kinase regulator activity / cellular response to insulin-like growth factor stimulus / positive regulation of DNA biosynthetic process / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / cochlea development / cellular response to platelet-derived growth factor stimulus / 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 / regulation of DNA replication / animal organ regeneration / post-translational protein modification / cellular response to estradiol stimulus / DNA Damage/Telomere Stress Induced Senescence / CDK-mediated phosphorylation and removal of Cdc6 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / Orc1 removal from chromatin / G1/S transition of mitotic cell cycle / G2/M transition of mitotic cell cycle / positive regulation of fibroblast proliferation / Regulation of TP53 Degradation / Processing of DNA double-strand break ends / Senescence-Associated Secretory Phenotype (SASP) / cellular response to hypoxia / Regulation of TP53 Activity through Phosphorylation / Ras protein signal transduction / Ub-specific processing proteases / protein domain specific binding / cell division / centrosome / DNA-templated transcription / positive regulation of DNA-templated transcription / protein kinase binding / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Jeffrey, P.D. / Russo, A.A. / Pavletich, N.P. | ||||||
Citation | Journal: Nature / Year: 1995 Title: Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Authors: Jeffrey, P.D. / Russo, A.A. / Polyak, K. / Gibbs, E. / Hurwitz, J. / Massague, J. / Pavletich, N.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fin.cif.gz | 239.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fin.ent.gz | 192.8 KB | Display | PDB format |
PDBx/mmJSON format | 1fin.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fin_validation.pdf.gz | 533.2 KB | Display | wwPDB validaton report |
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Full document | 1fin_full_validation.pdf.gz | 593.3 KB | Display | |
Data in XML | 1fin_validation.xml.gz | 31.2 KB | Display | |
Data in CIF | 1fin_validation.cif.gz | 48.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fi/1fin ftp://data.pdbj.org/pub/pdb/validation_reports/fi/1fin | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 33976.488 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: SF9 / Plasmid: PET3A / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 References: UniProt: P24941, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor #2: Protein | Mass: 29867.512 Da / Num. of mol.: 2 / Fragment: RESIDUES 173 - 432 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Description: THE FRAGMENT USED IN THE CRYSTALLIZATION WAS PRODUCED BY THE CLEAVAGE OF FULL-LENGTH CYCLIN A BY SUBTILISIN Cell line: SF9 / Plasmid: PET3A / Production host: Escherichia coli (E. coli) / Strain (production host): SF9 / References: UniProt: P20248 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.16 Å3/Da / Density % sol: 70 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.92 |
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Detector | Detector: CCD / Date: Feb 10, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Num. obs: 86466 / % possible obs: 90.2 % / Redundancy: 7.8 % / Rmerge(I) obs: 0.061 |
Reflection | *PLUS Highest resolution: 2.3 Å / Num. measured all: 677413 |
-Processing
Software |
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Refinement | Resolution: 2.3→6 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.208 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |