3SUR
Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline.
Summary for 3SUR
Entry DOI | 10.2210/pdb3sur/pdb |
Related | 3SUS 3SUT 3SUU 3SUV 3SUW |
Descriptor | Beta-hexosaminidase, SULFATE ION, 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 | structural genomics, riken structural genomics/proteomics initiative, rsgi, tim barrel, hydrolase, carbohydrate/sugar binding |
Biological source | Paenibacillus |
Total number of polymer chains | 1 |
Total formula weight | 57881.43 |
Authors | Sumida, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2011-07-11, release date: 2012-06-06, Last modification date: 2024-10-09) |
Primary citation | Sumida, T.,Stubbs, K.A.,Ito, M.,Yokoyama, S. Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach Org.Biomol.Chem., 10:2607-2612, 2012 Cited by PubMed Abstract: One useful methodology that has been used to give insight into how chemically synthesized inhibitors bind to enzymes and the reasons underlying their potency is crystallographic studies of inhibitor-enzyme complexes. Presented here is the X-ray structural analysis of a representative family 20 exo-β-N-acetylhexosaminidase in complex with various known classes of inhibitor of these types of enzymes, which highlights how different inhibitor classes can inhibit the same enzyme. This study will aid in the future development of inhibitors of not only exo-β-N-acetylhexosaminidases but also other types of glycoside hydrolases. PubMed: 22367352DOI: 10.1039/c2ob06636j PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report