Wildtype Streptomyces plicatus beta-hexosaminidase in complex with product (GlcNAc)

Summary for 1M01

Related1M03 1M04 1hp5 1jak
DescriptorBeta-N-acetylhexosaminidase, N-ACETYL-D-GLUCOSAMINE, CHLORIDE ION, ... (6 entities in total)
Functional Keywordssubstrate assisted catalysis, streptomyces plicatus, hexosaminidase, tim barrel, hydrolase
Biological sourceStreptomyces plicatus
Total number of polymer chains1
Total molecular weight56826.69
J Williams, S.,Mark, B.L.,Vocadlo, D.J.,James, M.N.G.,Withers, S.G. (deposition date: 2002-06-11, release date: 2003-01-21, Last modification date: 2011-07-13)
Primary citation
Williams, S.J.,Mark, B.L.,Vocadlo, D.J.,James, M.N.,Withers, S.G.
Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state.
J.Biol.Chem., 277:40055-40065, 2002
PubMed: 12171933 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M206481200
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.206500.8%1.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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