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PDBsum entry 2bkz

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2bkz
Jmol
Contents
Protein chains
302 a.a. *
257 a.a. *
Ligands
SBC ×2
SO4 ×2
Waters ×272
* Residue conservation analysis
PDB id:
2bkz
Name: Transferase
Title: Structure of cdk2-cyclin a with pha-404611
Structure: Cell division protein kinase 2. Chain: a, c. Synonym: p33 protein kinase. Engineered: yes. Cyclin a2. Chain: b, d. Fragment: residues 174-432 (c-terminal portion). Synonym: cyclin a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: highfive. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Biol. unit: Dimer (from PDB file)
Resolution:
2.6Å     R-factor:   0.230     R-free:   0.259
Authors: R.Dalessio,A.Bargiottia,S.Metz,M.G.Brasca,A.Cameron, A.Ermoli,A.Marsiglio,P.Polucci,F.Roletto,M.Tibolla, M.L.Vazquez,A.Vulpetti,P.Pevarello
Key ref: R.D'Alessio et al. (2005). Benzodipyrazoles: a new class of potent CDK2 inhibitors. Bioorg Med Chem Lett, 15, 1315-1319. PubMed id: 15713378 DOI: 10.1016/j.bmcl.2005.01.023
Date:
23-Feb-05     Release date:   08-Mar-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2
Seq:
Struc:
298 a.a.
302 a.a.
Protein chains
Pfam   ArchSchema ?
P20248  (CCNA2_HUMAN) -  Cyclin-A2
Seq:
Struc:
432 a.a.
257 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, C: E.C.2.7.11.22  - Cyclin-dependent kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cyclin-dependent protein kinase holoenzyme complex   15 terms 
  Biological process     regulation of gene silencing   30 terms 
  Biochemical function     nucleotide binding     13 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.bmcl.2005.01.023 Bioorg Med Chem Lett 15:1315-1319 (2005)
PubMed id: 15713378  
 
 
Benzodipyrazoles: a new class of potent CDK2 inhibitors.
R.D'Alessio, A.Bargiotti, S.Metz, M.G.Brasca, A.Cameron, A.Ermoli, A.Marsiglio, P.Polucci, F.Roletto, M.Tibolla, M.L.Vazquez, A.Vulpetti, P.Pevarello.
 
  ABSTRACT  
 
The synthesis and the preliminary expansion of this new class of CDK2 inhibitors are presented. The synthesis was accomplished using a solution-phase protocol amenable to rapid parallel expansion and suitable to be scaled-up in view of possible lead development. Following a medicinal chemistry program aimed at improving cell permeability and selectivity, a series of compounds with nanomolar activity in the biochemical assay and able to efficiently inhibit tumor cell proliferation has been obtained.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17571187 F.Marchetti, K.L.Sayle, J.Bentley, W.Clegg, N.J.Curtin, J.A.Endicott, B.T.Golding, R.J.Griffin, K.Haggerty, R.W.Harrington, V.Mesguiche, D.R.Newell, M.E.Noble, R.J.Parsons, D.J.Pratt, L.Z.Wang, and I.R.Hardcastle (2007).
Structure-based design of 2-arylamino-4-cyclohexylmethoxy-5-nitroso-6-aminopyrimidine inhibitors of cyclin-dependent kinase 2.
  Org Biomol Chem, 5, 1577-1585.  
17450625 M.G.Brasca, C.Albanese, R.Amici, D.Ballinari, L.Corti, V.Croci, D.Fancelli, F.Fiorentini, M.Nesi, P.Orsini, F.Orzi, W.Pastori, E.Perrone, E.Pesenti, P.Pevarello, F.Riccardi-Sirtori, F.Roletto, P.Roussel, M.Varasi, A.Vulpetti, and C.Mercurio (2007).
6-Substituted Pyrrolo[3,4-c]pyrazoles: An Improved Class of CDK2 Inhibitors.
  ChemMedChem, 2, 841-852.  
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