2LTJ
Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae
Summary for 2LTJ
Entry DOI | 10.2210/pdb2ltj/pdb |
NMR Information | BMRB: 18484 |
Descriptor | Beta-N-acetylhexosaminidase (1 entity in total) |
Functional Keywords | elongated, b-sheet, hydrolase |
Biological source | Streptococcus pneumoniae |
Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P49610 |
Total number of polymer chains | 1 |
Total formula weight | 12292.64 |
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 citation | Pluvinage, 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: 23154168DOI: 10.1016/j.jmb.2012.11.005 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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