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PDBsum entry 3tnw

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protein ligands metals Protein-protein interface(s) links
Transferase/transferase inhibitor PDB id
3tnw
Jmol
Contents
Protein chains
296 a.a.
257 a.a.
Ligands
F18 ×2
Metals
_NA ×2
Waters ×912
PDB id:
3tnw
Name: Transferase/transferase inhibitor
Title: Structure of cdk2/cyclin a in complex with can508
Structure: Cyclin-dependent kinase 2. Chain: a, c. Synonym: cell division protein kinase 2, p33 protein kinase engineered: yes. Cyclin-a2. Chain: b, d. Fragment: cyclin boxes, unp resdiues 169-430. Synonym: cyclin-a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cdk2. Expressed in: escherichia coli. Expression_system_taxid: 562. Bos taurus. Bovine. Organism_taxid: 9913.
Resolution:
2.00Å     R-factor:   0.188     R-free:   0.227
Authors: S.Baumli,A.J.Hole,J.A.Endicott
Key ref: S.Baumli et al. (2012). The CDK9 C-helix exhibits conformational plasticity that may explain the selectivity of CAN508. ACS Chem Biol, 7, 811-816. PubMed id: 22292676
Date:
02-Sep-11     Release date:   15-Feb-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P24941  (CDK2_HUMAN) -  Cyclin-dependent kinase 2
Seq:
Struc:
298 a.a.
296 a.a.*
Protein chains
Pfam   ArchSchema ?
P30274  (CCNA2_BOVIN) -  Cyclin-A2
Seq:
Struc:
430 a.a.
257 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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    
 
 
ACS Chem Biol 7:811-816 (2012)
PubMed id: 22292676  
 
 
The CDK9 C-helix exhibits conformational plasticity that may explain the selectivity of CAN508.
S.Baumli, A.J.Hole, M.E.Noble, J.A.Endicott.
 
  ABSTRACT  
 
No abstract given.