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PDBsum entry 4a55

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protein ligands Protein-protein interface(s) links
Transferase PDB id
4a55
Jmol
Contents
Protein chains
1001 a.a.
141 a.a.
Ligands
P08 ×2
PDB id:
4a55
Name: Transferase
Title: Crystal structure of p110alpha in complex with ish2 of p85al the inhibitor pik-108
Structure: Phosphatidylinositol-4,5-bisphosphate 3-kinase ca subunit alpha isoform. Chain: a. Synonym: pi3-kinase subunit alpha, pi3k-alpha, pi3kalpha, ptdins-3-kinase subunit alpha, phosphatidylinositol-4\,5-bisphosphate 3-kinase 110 kda ca subunit alpha, ptdins-3-kinase subunit p110-alpha, p110alp phosphoinositide-3-kinase catalytic alpha polypeptide, serine/threonine protein kinase pik3ca.
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Homo sapiens. Human. Organism_taxid: 9606.
Resolution:
3.50Å     R-factor:   0.185     R-free:   0.227
Authors: W.-C.Hon,A.Berndt,R.L.Williams
Key ref: W.C.Hon et al. (2012). Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases. Oncogene, 31, 3655-3666. PubMed id: 22120714 DOI: 10.1038/onc.2011.532
Date:
24-Oct-11     Release date:   28-Dec-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P42337  (PK3CA_MOUSE) -  Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1068 a.a.
1001 a.a.
Protein chain
Pfam   ArchSchema ?
P27986  (P85A_HUMAN) -  Phosphatidylinositol 3-kinase regulatory subunit alpha
Seq:
Struc:
 
Seq:
Struc:
724 a.a.
141 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: Chain A: E.C.2.7.1.153  - Phosphatidylinositol-4,5-bisphosphate 3-kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
1-Phosphatidyl-myo-inositol Metabolism
      Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP
+ 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
= ADP
+ 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
   Enzyme class 3: Chain A: E.C.2.7.11.1  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plasma membrane   4 terms 
  Biological process     phosphatidylinositol-3-phosphate biosynthetic process   16 terms 
  Biochemical function     nucleotide binding     14 terms  

 

 
    reference    
 
 
DOI no: 10.1038/onc.2011.532 Oncogene 31:3655-3666 (2012)
PubMed id: 22120714  
 
 
Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases.
W.C.Hon, A.Berndt, R.L.Williams.
 
  ABSTRACT  
 
No abstract given.