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PDBsum entry 3e8e

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3e8e
Jmol
Contents
Protein chains
(+ 0 more) 344 a.a. *
(+ 0 more) 20 a.a. *
Ligands
G98 ×6
Waters ×336
* Residue conservation analysis
PDB id:
3e8e
Name: Transferase
Title: Crystal structures of the kinase domain of pka in complex wi competitive inhibitors
Structure: Camp-dependent protein kinase catalytic subunit a chain: a, b, e, i, l, p. Fragment: camp-dependent pka kinase domain. Synonym: pka c-alpha. Engineered: yes. Pki inhibitor peptide. Chain: g, c, f, j, n, q. Engineered: yes
Source: Bos taurus. Cow. Organism_taxid: 9913. Gene: pka, prkaca. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide was chemically synthesized. It i naturally in bovine.
Resolution:
2.00Å     R-factor:   0.245     R-free:   0.279
Authors: N.O.Concha,P.A.Elkins,A.Smallwood,P.Ward
Key ref: M.B.Rouse et al. (2009). Aminofurazans as potent inhibitors of AKT kinase. Bioorg Med Chem Lett, 19, 1508-1511. PubMed id: 19179070
Date:
19-Aug-08     Release date:   18-Nov-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00517  (KAPCA_BOVIN) -  cAMP-dependent protein kinase catalytic subunit alpha
Seq:
Struc:
351 a.a.
344 a.a.*
Protein chains
Pfam   ArchSchema ?
Q3SX13  (IPKA_BOVIN) -  cAMP-dependent protein kinase inhibitor alpha
Seq:
Struc:
76 a.a.
20 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, B, E, I, L, P: E.C.2.7.11.11  - cAMP-dependent protein 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     sperm midpiece   11 terms 
  Biological process     regulation of proteasomal protein catabolic process   18 terms 
  Biochemical function     nucleotide binding     13 terms  

 

 
    reference    
 
 
Bioorg Med Chem Lett 19:1508-1511 (2009)
PubMed id: 19179070  
 
 
Aminofurazans as potent inhibitors of AKT kinase.
M.B.Rouse, M.A.Seefeld, J.D.Leber, K.C.McNulty, L.Sun, W.H.Miller, S.Zhang, E.A.Minthorn, N.O.Concha, A.E.Choudhry, M.D.Schaber, D.A.Heerding.
 
  ABSTRACT  
 
AKT inhibitors containing an imidazopyridine aminofurazan scaffold have been optimized. We have previously disclosed identification of the AKT inhibitor GSK690693, which has been evaluated in clinical trials in cancer patients. Herein we describe recent efforts focusing on investigating a distinct region of this scaffold that have afforded compounds (30 and 32) with comparable activity profiles to that of GSK690693.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19912230 M.Congreve, and F.Marshall (2010).
The impact of GPCR structures on pharmacology and structure-based drug design.
  Br J Pharmacol, 159, 986-996.  
20151677 T.McHardy, J.J.Caldwell, K.M.Cheung, L.J.Hunter, K.Taylor, M.Rowlands, R.Ruddle, A.Henley, A.de Haven Brandon, M.Valenti, T.G.Davies, L.Fazal, L.Seavers, F.I.Raynaud, S.A.Eccles, G.W.Aherne, M.D.Garrett, and I.Collins (2010).
Discovery of 4-amino-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidine-4-carboxamides as selective, orally active inhibitors of protein kinase B (Akt).
  J Med Chem, 53, 2239-2249.
PDB codes: 2x37 2x39 2xh5
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.