3ZFQ

Crystal structure of product-like, processed N-terminal protease Npro with mercury

Summary for 3ZFQ

Related3ZFN 3ZFO 3ZFP 3ZFR 3ZFT 3ZFU
DescriptorN-TERMINAL PROTEASE NPRO, MONOTHIOGLYCEROL, MERCURY (II) ION, ... (4 entities in total)
Functional Keywordshydrolase, auto-processing cysteine protease, viral protease, in cis- cleavage, hydroxide-dependent catalysis, auto-proteolysis, immune modulation, host-pathogen interaction, convergent evolution
Biological sourcePESTIVIRUS STRAIN D32/00_HOBI
Total number of polymer chains1
Total molecular weight16866.78
Authors
Zogg, T.,Sponring, M.,Schindler, S.,Koll, M.,Schneider, R.,Brandstetter, H.,Auer, B. (deposition date: 2012-12-12, release date: 2013-05-15, Last modification date: 2017-07-05)
Primary citation
Zogg, T.,Sponring, M.,Schindler, S.,Koll, M.,Schneider, R.,Brandstetter, H.,Auer, B.
Crystal Structures of the Viral Protease Npro Imply Distinct Roles for the Catalytic Water in Catalysis
Structure, 21:929-, 2013
PubMed: 23643950 (PDB entries with the same primary citation)
DOI: 10.1016/J.STR.2013.04.003
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.65 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.28541.4%3.9%2.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution