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PDBsum entry 3pvg

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protein ligands links
Transferase/transferase inhibitor PDB id
3pvg

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
327 a.a. *
Ligands
K68
Waters ×279
* Residue conservation analysis
PDB id:
3pvg
Name: Transferase/transferase inhibitor
Title: Crystal structure of z. Mays ck2 alpha subunit in complex with the inhibitor 4,5,6,7-tetrabromo-1-carboxymethylbenzimidazole (k68)
Structure: Casein kinase ii subunit alpha. Chain: a. Fragment: alpha subunit. Synonym: ck ii, ck2-alpha. Engineered: yes
Source: Zea mays. Maize. Organism_taxid: 4577. Gene: ack2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.50Å     R-factor:   0.183     R-free:   0.211
Authors: E.Papinutto,C.Franchin,R.Battistutta
Key ref: S.Sarno et al. (2011). ATP site-directed inhibitors of protein kinase CK2: an update. Curr Top Med Chem, 11, 1340-1351. PubMed id: 21513497
Date:
07-Dec-10     Release date:   15-Dec-10    
Supersedes: 3kxj
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P28523  (CSK2A_MAIZE) -  Casein kinase II subunit alpha from Zea mays
Seq:
Struc:
332 a.a.
327 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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    
 
 
Curr Top Med Chem 11:1340-1351 (2011)
PubMed id: 21513497  
 
 
ATP site-directed inhibitors of protein kinase CK2: an update.
S.Sarno, E.Papinutto, C.Franchin, J.Bain, M.Elliott, F.Meggio, Z.Kazimierczuk, A.Orzeszko, G.Zanotti, R.Battistutta, L.A.Pinna.
 
  ABSTRACT  
 
No abstract given.

 

 

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