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1L30

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY

Summary for 1L30
Entry DOI10.2210/pdb1l30/pdb
Related1L01 1L02 1L03 1L04 1L05 1L06 1L07 1L08 1L09 1L10 1L11 1L12 1L13 1L14 1L15 1L16 1L17 1L18 1L19 1L20 1L21 1L22 1L23 1L24 1L25 1L26 1L27 1L28 1L29 1L31 1L32 1L33 1L34 1L35 1L36 2LZM
DescriptorT4 LYSOZYME (2 entities in total)
Functional Keywordshydrolase (o-glycosyl)
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm : P00720
Total number of polymer chains1
Total formula weight18678.51
Authors
Bell, J.A.,Dao-Pin, S.,Matthews, B.W. (deposition date: 1989-05-01, release date: 1990-01-15, Last modification date: 2022-11-23)
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
Cited by
PubMed: 3277275
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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