1FVJ

THE 2.06 ANGSTROM STRUCTURE OF THE H32Y MUTANT OF THE DISULFIDE BOND FORMATION PROTEIN (DSBA)

Summary for 1FVJ

DescriptorDISULFIDE BOND FORMATION PROTEIN (2 entities in total)
Functional Keywordsprotein disulfide isomerase, protein folding, redox protein disulfide oxidoreductase, disulfide oxidoreductase
Biological sourceEscherichia coli
Total number of polymer chains2
Total molecular weight42360.11
Authors
Martin, J.L.,Guddat, L.W. (deposition date: 1996-08-28, release date: 1997-05-15, Last modification date: 2011-07-13)
Primary citation
Guddat, L.W.,Bardwell, J.C.,Glockshuber, R.,Huber-Wunderlich, M.,Zander, T.,Martin, J.L.
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
Protein Sci., 6:1893-1900, 1997
PubMed: 9300489 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.06 Å)
NMR Information
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.215204.6%2.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution