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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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( jV3 / Jmol ) *1
PDB ID1ctw  sequence information (FASTA format)   
RELATED PDB ID1cu0, 1cu2, 1cu3, 1cu6, 1cu5, 1cup, 1cuq, 1cv0, 1cv1, 1qsq, 1cv4, 1cv3, 1cv5, 1cv6, 1cvk, 1d2w, 1d2y, 1d3f, 1d3j
DescriptorLYSOZYME (E.C.3.2.1.17)
TitleT4 LYSOZYME MUTANT I78A
Functional KeywordsHYDROLASE (O-GLYCOSYL), T4 LYSOZYME, CAVITY MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING
Biological sourceEnterobacteria phage T4
Total number of polymer chains1
Total molecular weight18776.1 (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 ( 2.1[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00720 ) , eF-site , KEGG ( EC 3.2.1.17 ) , PISA