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2LTJ

Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae

Summary for 2LTJ
Entry DOI10.2210/pdb2ltj/pdb
NMR InformationBMRB: 18484
DescriptorBeta-N-acetylhexosaminidase (1 entity in total)
Functional Keywordselongated, b-sheet, hydrolase
Biological sourceStreptococcus pneumoniae
Cellular locationSecreted, cell wall; Peptidoglycan-anchor (Potential): P49610
Total number of polymer chains1
Total formula weight12292.64
Authors
Pluvinage, B.,Chitayat, S.,Ficko-Blean, E.,Abbott, D.,Kunjachen, J.,Grondin, J.,Spencer, H.,Smith, S.,Boraston, A. (deposition date: 2012-05-28, release date: 2012-11-28, Last modification date: 2013-06-19)
Primary citationPluvinage, B.,Chitayat, S.,Ficko-Blean, E.,Abbott, D.W.,Kunjachen, J.M.,Grondin, J.,Spencer, H.L.,Smith, S.P.,Boraston, A.B.
Conformational analysis of StrH, the surface-attached exo-beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae.
J.Mol.Biol., 425:334-349, 2013
Cited by
PubMed: 23154168
DOI: 10.1016/j.jmb.2012.11.005
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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