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PDBsum entry 4ja7

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protein metals links
Hydrolase PDB id
4ja7

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
466 a.a.
Metals
_MG ×2
Waters ×106
PDB id:
4ja7
Name: Hydrolase
Title: Rat pp5 co-crystallized with p5sa-2
Structure: Serine/threonine-protein phosphatase 5. Chain: a. Synonym: pp5, protein phosphatase t, ppt. Engineered: yes
Source: Rattus norvegicus. Brown rat,rat,rats. Organism_taxid: 10116. Gene: ppp5c. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.00Å     R-factor:   0.216     R-free:   0.262
Authors: V.Haslbeck,M.Helmuth,F.Alte,G.Popowicz,W.Schmidt,M.Weiwad,G.Fischer, G.Gemmecker,M.Sattler,F.Striggow,M.Groll,K.Richter
Key ref: V.Haslbeck et al. (2015). Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism. Biosci Rep, 35, . PubMed id: 26182372 DOI: 10.1042/BSR20150042
Date:
18-Feb-13     Release date:   19-Feb-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P53042  (PPP5_RAT) -  Serine/threonine-protein phosphatase 5 from Rattus norvegicus
Seq:
Struc:
499 a.a.
466 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.16  - protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
O-phospho-L-seryl-[protein]
+ H2O
= L-seryl-[protein]
+ phosphate
O-phospho-L-threonyl-[protein]
+ H2O
= L-threonyl-[protein]
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1042/BSR20150042 Biosci Rep 35: (2015)
PubMed id: 26182372  
 
 
Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism.
V.Haslbeck, A.Drazic, J.M.Eckl, F.Alte, M.Helmuth, G.Popowicz, W.Schmidt, F.Braun, M.Weiwad, G.Fischer, G.Gemmecker, M.Sattler, F.Striggow, M.Groll, K.Richter.
 
  ABSTRACT  
 
No abstract given.

 

 

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