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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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PDB ID1l25  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, 1l23, 1l24, 1l26, 1l27, 1l28, 1l29, 1l30, 1l31, 1l32, 1l33, 1l34, 1l35, 1l36
DescriptorLYSOZYME (E.C.3.2.1.17) (MUTANT WITH PRO 86 REPLACED BY ALA) (P86A)
TitleREPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY
Functional KeywordsHYDROLASE (O-GLYCOSYL)
Biological sourceEnterobacteria phage T4
Organ sourceEGG
Total number of polymer chains1
Total molecular weight18636.6 (the details in Structural Details Page)
AuthorsBell, J.A. , Dao-Pin, S. , Matthews, B.W. (deposition date : 1989-05-01, release date : 1990-01-15)
Primary citationAlber, T. , Bell, J.A. , Sun, D.P. , Nicholson, H. , Wozniak, J.A. , Cook, S. , Matthews, B.W.
Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Science, 239:631 - 635, 1988.(PubMed : 3277275)
Experimental methodX-RAY DIFFRACTION ( 1.8[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00720 ) , eF-site , KEGG ( EC 3.2.1.17 ) , PISA