1CU0
T4 LYSOZYME MUTANT I78M
Summary for 1CU0
Entry DOI | 10.2210/pdb1cu0/pdb |
Related | 1CTW 1CU2 1CU3 1CU5 1CU6 1CUP 1CUQ 1CV0 1CV1 1CV3 1CV4 1CV5 1CV6 1CVK 1D2W 1D2Y 1D3F 1D3J 1QSQ |
Descriptor | LYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total) |
Functional Keywords | hydrolase (o-glycosyl), t4 lysozyme, methionine core mutant, protein engineering, protein folding, hydrolase |
Biological source | Enterobacteria phage T4 |
Cellular location | Host cytoplasm : P00720 |
Total number of polymer chains | 1 |
Total formula weight | 18871.56 |
Authors | Gassner, N.C.,Baase, W.A.,Lindstrom, J.D.,Lu, J.,Matthews, B.W. (deposition date: 1999-08-20, release date: 1999-11-10, Last modification date: 2024-02-07) |
Primary citation | Gassner, 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 Cited by PubMed: 10545167DOI: 10.1021/bi9915519 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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