Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5EHT

Indirect contributions of mutations underlie optimization of new enzyme function

Summary for 5EHT
Entry DOI10.2210/pdb5eht/pdb
Related5EH9
DescriptorN-acyl homoserine lactonase, ZINC ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsn-acyl-homoserine lactonase, directed evolution, aiia, qql, lactonase, phosphatase, paraoxonase, hydrolase
Biological sourceBacillus thuringiensis
Total number of polymer chains1
Total formula weight29151.71
Authors
Jackson, C.J.,Hong, N.-S. (deposition date: 2015-10-28, release date: 2016-09-07, Last modification date: 2023-11-15)
Primary citationYang, G.,Hong, N.,Baier, F.,Jackson, C.J.,Tokuriki, N.
Conformational Tinkering Drives Evolution of a Promiscuous Activity through Indirect Mutational Effects.
Biochemistry, 55:4583-4593, 2016
Cited by
PubMed: 27444875
DOI: 10.1021/acs.biochem.6b00561
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.29 Å)
Structure validation

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon