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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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PDB ID189l  sequence information (FASTA format)   
DescriptorLYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 3 REPLACED BY LEU, SER 38 REPLACED BY ASP, ALA 41 REPLACED BY VAL, ALA 82 PRO, ASN 116 REPLACED BY ASP, VAL 131 REPLACED BY ALA, AND ASN 144 REPLACED BY ASP SUBSTITUTIONS (I3L,S38D,A41V, A82P,N116D,V131A,N144D)
TitleENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE
Functional KeywordsHYDROLASE (O-GLYCOSYL)
Biological sourceEnterobacteria phage T4
Total number of polymer chains1
Total molecular weight18718.6 (the details in Structural Details Page)
AuthorsZhang, X.-J. , Matthews, B.W. (deposition date : 1995-05-09, release date : 1995-07-31)
Primary citationZhang, X.J. , Baase, W.A. , Shoichet, B.K. , Wilson, K.P. , Matthews, B.W.
Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive.
Protein Eng., 8:1017 - 1022, 1995.(PubMed : 8771182)  (DOI: 10.1093/protein/8.10.1017)
Experimental methodX-RAY DIFFRACTION ( 2.5[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00720 ) , eF-site , KEGG ( EC 3.2.1.17 ) , PISA