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PDBsum entry 4xaz

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4xaz

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
328 a.a.
Ligands
MPD
Metals
_ZN ×4
Waters ×581
PDB id:
4xaz
Name: Hydrolase
Title: Cycles of destabilization and repair underlie evolutionary transitions in enzymes
Structure: Phosphotriesterase variant pte-r18. Chain: a, g. Engineered: yes
Source: Brevundimonas diminuta. Organism_taxid: 293. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.55Å     R-factor:   0.175     R-free:   0.206
Authors: C.J.Jackson,E.Campbell,M.Kaltenbach,N.Tokuriki
Key ref: E.Campbell et al. (2016). The role of protein dynamics in the evolution of new enzyme function. Nat Chem Biol, 12, 944-950. PubMed id: 27618189 DOI: 10.1038/nchembio.2175
Date:
16-Dec-14     Release date:   16-Dec-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0A060GYS7  (A0A060GYS7_BREDI) -  Phosphotriesterase variant PTE-R18 from Brevundimonas diminuta
Seq:
Struc:
333 a.a.
328 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1038/nchembio.2175 Nat Chem Biol 12:944-950 (2016)
PubMed id: 27618189  
 
 
The role of protein dynamics in the evolution of new enzyme function.
E.Campbell, M.Kaltenbach, G.J.Correy, P.D.Carr, B.T.Porebski, E.K.Livingstone, L.Afriat-Jurnou, A.M.Buckle, M.Weik, F.Hollfelder, N.Tokuriki, C.J.Jackson.
 
  ABSTRACT  
 
No abstract given.

 

 

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