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1CV1

T4 LYSOZYME MUTANT V111M

Summary for 1CV1
Entry DOI10.2210/pdb1cv1/pdb
Related1CTW 1CU0 1CU2 1CU3 1CU5 1CU6 1CUP 1CUQ 1CV0 1CV3 1CV4 1CV5 1CV6 1CVK 1D2W 1D2Y 1D3F 1D3J 1QSQ
DescriptorLYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total)
Functional Keywordshydrolase (o-glycosyl), t4 lysozyme, methionine core mutant, protein engineering, protein folding, hydrolase
Biological sourceEnterobacteria phage T4
Total number of polymer chains1
Total formula weight18885.58
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 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 (2.1 Å)
Structure validation

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