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MineSummary [1l23]

Summary Structural Experimental Function Sequence Neighbor Download Link

<Asymmetric unit>
= <Biological unit>

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( jV3 / Jmol ) *1
PDB ID1l23  sequence information (FASTA format)   
RELATED PDB ID2lzm, 1l01, 1l02, 1l03, 1l04, 1l05, 1l06, 1l07, 1l08, 1l09, 1l10, 1l11, 1l12, 1l13, 1l14, 1l15, 1l16, 1l17, 1l18, 1l19, 1l20, 1l21, 1l22, 1l24, 1l25, 1l26, 1l27, 1l28, 1l29, 1l30, 1l31, 1l32, 1l33, 1l34, 1l35, 1l36
DescriptorLYSOZYME (E.C.3.2.1.17) (MUTANT WITH GLY 77 REPLACED BY ALA) (G77A)
TitleENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Functional KeywordsHYDROLASE (O-GLYCOSYL)
Biological sourceEnterobacteria phage T4
Organ sourceEGG
Total number of polymer chains1
Total molecular weight18676.6 (the details in Structural Details Page)
AuthorsNicholson, H. , Matthews, B.W. (deposition date : 1989-05-01, release date : 1990-01-15)
Primary citationMatthews, B.W. , Nicholson, H. , Becktel, W.J.
Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Proc. Natl. Acad. Sci. U.S.A., 84:6663 - 6667, 1987.(PubMed : 3477797)  (DOI: 10.1073/pnas.84.19.6663)
Experimental methodX-RAY DIFFRACTION ( 1.7[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00720 ) , eF-site , KEGG ( EC 3.2.1.17 ) , PISA