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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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( jV3 / Jmol ) *1
PDB ID1cv0  sequence information (FASTA format)   
RELATED PDB ID1ctw, 1cu0, 1cu2, 1cu3, 1cu6, 1cu5, 1cup, 1cuq, 1cv1, 1qsq, 1cv4, 1cv3, 1cv5, 1cv6, 1cvk, 1d2w, 1d2y, 1d3f, 1d3j
DescriptorLYSOZYME (E.C.3.2.1.17)
TitleT4 LYSOZYME MUTANT F104M
Functional KeywordsHYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING
Biological sourceEnterobacteria phage T4
Total number of polymer chains1
Total molecular weight18837.7 (the details in Structural Details Page)
AuthorsGassner, N.C. , Baase, W.A. , Lindstrom, J.D. , Lu, J. , Matthews, B.W. (deposition date : 1999-08-20, release date : 1999-11-10)
Primary citationGassner, N.C. , Baase, W.A. , Lindstrom, J.D. , Lu, J. , Dahlquist, F.W. , Matthews, B.W.
Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Biochemistry, 38:14451 - 14460, 1999.(PubMed : 10545167)  (DOI: 10.1021/bi9915519)
Experimental methodX-RAY DIFFRACTION ( 2.12[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00720 ) , eF-site , KEGG ( EC 3.2.1.17 ) , PISA