4QDN
Crystal Structure of the endo-beta-N-acetylglucosaminidase from Thermotoga maritima
Summary for 4QDN
Entry DOI | 10.2210/pdb4qdn/pdb |
Descriptor | Flagellar protein FlgJ [peptidoglycan hydrolase], PHOSPHATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
Functional Keywords | gh73 family (cazy database), inverting mechanism, bacterial peptidoglycan hydrolysis, typical lysozyme alpha-beta fold with only the alpha-lobe, glycoside hydrolase, hydrolase |
Biological source | Thermotoga maritima |
Total number of polymer chains | 1 |
Total formula weight | 16059.31 |
Authors | Lipski, A.,Nurizzo, D.,Bourne, Y.,Vincent, F. (deposition date: 2014-05-14, release date: 2014-11-12, Last modification date: 2024-02-28) |
Primary citation | Lipski, A.,Herve, M.,Lombard, V.,Nurizzo, D.,Mengin-Lecreulx, D.,Bourne, Y.,Vincent, F. Structural and biochemical characterization of the beta-N-acetylglucosaminidase from Thermotoga maritima: Toward rationalization of mechanistic knowledge in the GH73 family. Glycobiology, 25:319-330, 2015 Cited by PubMed: 25344445DOI: 10.1093/glycob/cwu113 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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