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1CU5

T4 LYSOZYME MUTANT L91M

Summary for 1CU5
Entry DOI10.2210/pdb1cu5/pdb
Related1CTW 1CU0 1CU2 1CU3 1CU5 1CUP 1CUQ 1CV0 1CV1 1CV3 1CV4 1CV5 1CV6 1CVK 1D2W 1D2Y 1D3F 1D3J 1QSQ
DescriptorLYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total)
Functional Keywordst4 lysoxyme, methionine core mutant, protein folding, hydrolase
Biological sourceEnterobacteria phage T4
Total number of polymer chains1
Total formula weight18871.56
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: 2024-02-14)
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
Cited by
PubMed: 10545167
DOI: 10.1021/bi9915519
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

217705

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