1NHQ

CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303

Summary for 1NHQ

DescriptorNADH PEROXIDASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
Functional Keywordsoxidoreductase (h2o2(a))
Biological sourceEnterococcus faecalis
Total number of polymer chains1
Total molecular weight50468.78
Authors
Mande, S.S.,Claiborne, A.,Hol, W.G.J. (deposition date: 1994-12-09, release date: 1995-02-14, Last modification date: 2012-03-28)
Primary citation
Mande, S.S.,Parsonage, D.,Claiborne, A.,Hol, W.G.
Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303.
Biochemistry, 34:6985-6992, 1995
PubMed: 7766608 (PDB entries with the same primary citation)
DOI: 10.1021/bi00021a010
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers20.2%6.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report