PDBsum entry 3nme

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Hydrolase PDB id
Protein chains
290 a.a. *
PO4 ×2
Waters ×196
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Structure of a plant phosphatase
Structure: Sex4 glucan phosphatase. Chain: a, b. Fragment: unp residues 90-379. Synonym: ptpkis1 protein. Engineered: yes. Mutation: yes
Source: Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: at3g52180. Expressed in: escherichia coli. Expression_system_taxid: 511693.
2.40Å     R-factor:   0.202     R-free:   0.250
Authors: C.W.Vander Kooi
Key ref: C.W.Vander Kooi et al. (2010). Structural basis for the glucan phosphatase activity of Starch Excess4. Proc Natl Acad Sci U S A, 107, 15379-15384. PubMed id: 20679247
22-Jun-10     Release date:   11-Aug-10    
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Protein chains
Pfam   ArchSchema ?
Q9FEB5  (DSP4_ARATH) -  Phosphoglucan phosphatase DSP4, chloroplastic
379 a.a.
290 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  


Proc Natl Acad Sci U S A 107:15379-15384 (2010)
PubMed id: 20679247  
Structural basis for the glucan phosphatase activity of Starch Excess4.
C.W.Vander Kooi, A.O.Taylor, R.M.Pace, D.A.Meekins, H.F.Guo, Y.Kim, M.S.Gentry.
No abstract given.


Literature references that cite this PDB file's key reference

  PubMed id Reference
  21294843 M.A.Glaring, M.J.Baumann, M.Abou Hachem, H.Nakai, N.Nakai, D.Santelia, B.W.Sigurskjold, S.C.Zeeman, A.Blennow, and B.Svensson (2011).
Starch-binding domains in the CBM45 family--low-affinity domains from glucan, water dikinase and α-amylase involved in plastidial starch metabolism.
  FEBS J, 278, 1175-1185.  
20724661 V.S.Tagliabracci, and P.J.Roach (2010).
Insights into the mechanism of polysaccharide dephosphorylation by a glucan phosphatase.
  Proc Natl Acad Sci U S A, 107, 15312-15313.  
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