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PDBsum entry 5mqh

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Transferase PDB id
5mqh

 

 

 

 

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Contents
Protein chain
228 a.a.
Waters ×33
PDB id:
5mqh
Name: Transferase
Title: Structure of the phosphatase domain of the cell fate determinant spoiie from bacillus subtilis in a crystal form without domain swapping
Structure: Serine phosphatase. Chain: a. Engineered: yes. Mutation: yes. Other_details: the mutation ala624 to ile was introduced to reduce successfully the extent of domain swapping.
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: sc09_contig28orf00413. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.45Å     R-factor:   0.214     R-free:   0.278
Authors: V.M.Levdikov,A.J.Wilkinson,E.V.Blagova
Key ref: N.Bradshaw et al. (2017). A widespread family of serine/threonine protein phosp shares a common regulatory switch with proteasomal proteases.. Elife, 6, . PubMed id: 28527238
Date:
20-Dec-16     Release date:   31-May-17    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P37475  (SP2E_BACSU) -  Stage II sporulation protein E from Bacillus subtilis (strain 168)
Seq:
Struc:
 
Seq:
Struc:
827 a.a.
228 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 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

 

 

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