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PDBsum entry 2xmy

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protein ligands links
Transferase PDB id
2xmy

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
295 a.a. *
Ligands
CDK
Waters ×255
* Residue conservation analysis
PDB id:
2xmy
Name: Transferase
Title: Discovery and characterisation of 2-anilino-4-(thiazol-5-yl) pyrimidine transcriptional cdk inhibitors as anticancer agents
Structure: Cell division protein kinase 2. Chain: a. Synonym: p33 protein kinase. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9.
Resolution:
1.90Å     R-factor:   0.192     R-free:   0.271
Authors: S.Wang,G.Griffiths,C.A.Midgley,A.L.Barnett,M.Cooper,J.Grabarek, L.Ingram,W.Jackson,G.Kontopidis,S.J.Mcclue,C.Mcinnes,J.Mclachlan, C.Meades,M.Mezna,I.Stuart,M.P.Thomas,D.I.Zheleva,D.P.Lane, R.C.Jackson,D.M.Glover,D.G.Blake,P.M.Fischer
Key ref: S.Wang et al. (2010). Discovery and characterization of 2-anilino-4- (thiazol-5-yl)pyrimidine transcriptional CDK inhibitors as anticancer agents. Chem Biol, 17, 1111-1121. PubMed id: 21035734
Date:
29-Jul-10     Release date:   10-Nov-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2 from Homo sapiens
Seq:
Struc:
298 a.a.
295 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.22  - cyclin-dependent kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Chem Biol 17:1111-1121 (2010)
PubMed id: 21035734  
 
 
Discovery and characterization of 2-anilino-4- (thiazol-5-yl)pyrimidine transcriptional CDK inhibitors as anticancer agents.
S.Wang, G.Griffiths, C.A.Midgley, A.L.Barnett, M.Cooper, J.Grabarek, L.Ingram, W.Jackson, G.Kontopidis, S.J.McClue, C.McInnes, J.McLachlan, C.Meades, M.Mezna, I.Stuart, M.P.Thomas, D.I.Zheleva, D.P.Lane, R.C.Jackson, D.M.Glover, D.G.Blake, P.M.Fischer.
 
  ABSTRACT  
 
No abstract given.

 

 

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