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PDBsum entry 3o96

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protein ligands links
Transferase PDB id
3o96

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
367 a.a. *
Ligands
IQO
Waters ×21
* Residue conservation analysis
PDB id:
3o96
Name: Transferase
Title: Crystal structure of human akt1 with an allosteric inhibitor
Structure: Rac-alpha serine/threonine-protein kinase. Chain: a. Fragment: unp residues 2-443. Synonym: rac-pk-alpha, protein kinase b, pkb, proto-oncogenE C-akt. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: akt1, pkb, rac. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: hi5 insect cells
Resolution:
2.70Å     R-factor:   0.249     R-free:   0.308
Authors: W.C.Voegtli,W.-I.Wu,H.A.Lord-Ondash,F.P.Dizon,G.P.A.Vigers, B.J.Brandhuber
Key ref: W.I.Wu et al. (2010). Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition. Plos One, 5, e12913-12913. PubMed id: 20886116
Date:
03-Aug-10     Release date:   13-Oct-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P31749  (AKT1_HUMAN) -  RAC-alpha serine/threonine-protein kinase from Homo sapiens
Seq:
Struc:
480 a.a.
367 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - non-specific serine/threonine protein 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    
 
 
Plos One 5:e12913-12913 (2010)
PubMed id: 20886116  
 
 
Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition.
W.I.Wu, W.C.Voegtli, H.L.Sturgis, F.P.Dizon, G.P.Vigers, B.J.Brandhuber.
 
  ABSTRACT  
 
No abstract given.

 

 

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