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PDBsum entry 7a0c

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protein ligands metals Protein-protein interface(s) links
Metal binding protein PDB id
7a0c

 

 

 

 

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Contents
Protein chains
498 a.a.
Ligands
QTT ×2
ACT ×9
GOL ×9
Metals
_MG ×5
_CL
_FE ×2
Waters ×795
PDB id:
7a0c
Name: Metal binding protein
Title: X-ray structure of nika from escherichia coli in complex with fe-6- me2-bpmcn
Structure: Nickel-binding periplasmic protein. Chain: a, b. Engineered: yes
Source: Escherichia coli (strain k12). Organism_taxid: 83333. Strain: k12. Gene: nika, b3476, jw3441. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
Resolution:
1.90Å     R-factor:   0.184     R-free:   0.222
Authors: C.Cavazza,S.Menage
Key ref: S.Lopez et al. (2020). A Selective Sulfide Oxidation Catalyzed by Heterogeneous Artificial Metalloenzymes Iron@NikA. Chemistry, 26, 16633-16638. PubMed id: 33079395 DOI: 10.1002/chem.202003746
Date:
07-Aug-20     Release date:   04-Nov-20    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P33590  (NIKA_ECOLI) -  Nickel-binding periplasmic protein from Escherichia coli (strain K12)
Seq:
Struc:
 
Seq:
Struc:
524 a.a.
498 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1002/chem.202003746 Chemistry 26:16633-16638 (2020)
PubMed id: 33079395  
 
 
A Selective Sulfide Oxidation Catalyzed by Heterogeneous Artificial Metalloenzymes Iron@NikA.
S.Lopez, C.Marchi-Delapierre, C.Cavazza, S.Ménage.
 
  ABSTRACT  
 
Performing a heterogeneous catalysis with proteins is still a challenge. Herein, we demonstrate the importance of cross-linked crystals for sulfoxide oxidation by an artificial enzyme. The biohybrid consists of the insertion of an iron complex into a NikA protein crystal. The heterogeneous catalysts displays a better efficiency-with higher reaction kinetics, a better stability and expand the substrate scope compared to its solution counterpart. Designing crystalline artificial enzymes represents a good alternative to soluble or supported enzymes for the future of synthetic biology.
 

 

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