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PDBsum entry 3uc3

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protein metals links
Transferase PDB id
3uc3

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
272 a.a.
Metals
_CO ×3
Waters ×143
PDB id:
3uc3
Name: Transferase
Title: The crystal structure of snf1-related kinase 2.3
Structure: Serine/threonine-protein kinase srk2i. Chain: a. Fragment: kinase domain. Synonym: ost1-kinase-like 2, protein athprokin b, snf1-related kinase 2.3, snrk2.3. Engineered: yes. Mutation: yes
Source: Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: srk2i, 41k, oskl2, snrk2.3, at5g66880, mud21.14. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.214     R-free:   0.230
Authors: X.E.Zhou,L.-M.Ng,F.-F.Soon,A.Kovach,K.M.Suino-Powell,J.Li,K.Melcher, H.E.Xu
Key ref: L.M.Ng et al. (2011). Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases. Proc Natl Acad Sci U S A, 108, 21259-21264. PubMed id: 22160701
Date:
25-Oct-11     Release date:   14-Dec-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q39193  (SRK2I_ARATH) -  Serine/threonine-protein kinase SRK2I from Arabidopsis thaliana
Seq:
Struc:
361 a.a.
272 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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    
 
 
Proc Natl Acad Sci U S A 108:21259-21264 (2011)
PubMed id: 22160701  
 
 
Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases.
L.M.Ng, F.F.Soon, X.E.Zhou, G.M.West, A.Kovach, K.M.Suino-Powell, M.J.Chalmers, J.Li, E.L.Yong, J.K.Zhu, P.R.Griffin, K.Melcher, H.E.Xu.
 
  ABSTRACT  
 
No abstract given.

 

 

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