1CVK

T4 LYSOZYME MUTANT L118A

Summary for 1CVK

Related1CTW 1CU0 1CU2 1CU3 1CU6 1CU5 1CUP 1CUQ 1CV0 1CV1 1QSQ 1CV4 1CV3 1CV5 1CV6 1CVK 1D2W 1D2Y 1D3F 1D3J
DescriptorLYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total)
Functional Keywordshydrolase (o-glycosyl), t4 lysozyme, cavity-forming mutant, protein engineering, protein folding, hydrolase
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm  P00720
Total number of polymer chains1
Total molecular weight18811.44
Authors
Gassner, N.C.,Baase, W.A.,Lindstrom, J.,Lu, J.,Matthews, B.W. (deposition date: 1999-08-23, release date: 1999-11-10, Last modification date: 2018-01-31)
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
PubMed: 10545167 (PDB entries with the same primary citation)
DOI: 10.1021/bi9915519
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers805.2%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report