5A6A
GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT
Summary for 5A6A
Entry DOI | 10.2210/pdb5a6a/pdb |
Related | 5A69 5A6B 5A6J 5A6K |
Descriptor | N-ACETYL-BETA-D-GLUCOSAMINIDASE, 1,2-ETHANEDIOL, 3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL, ... (4 entities in total) |
Functional Keywords | hydrolase, beta-hexosaminidase, streptococcus pneumoniae, bacterial proteins, carbohydrate conformation, catalytic domain, enzyme inhibitors, host-pathogen interactions, hydrogen bonding, hydrolysis, models, polysaccharides, protein binding, virulence factors |
Biological source | STREPTOCOCCUS PNEUMONIAE |
Total number of polymer chains | 2 |
Total formula weight | 148863.62 |
Authors | Cid, M.,Robb, C.S.,Higgins, M.A.,Boraston, A.B. (deposition date: 2015-06-24, release date: 2015-09-23, Last modification date: 2024-01-10) |
Primary citation | Robb, M.,Robb, C.S.,Higgins, M.A.,Hobbs, J.K.,Paton, J.C.,Boraston, A.B. A Second beta-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans. J. Biol. Chem., 290:30888-30900, 2015 Cited by PubMed: 26491009DOI: 10.1074/jbc.M115.688630 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.69 Å) |
Structure validation
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