1C82
MECHANISM OF HYALURONAN BINDING AND DEGRADATION: STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH HYALURONIC ACID DISACCHARIDE AT 1.7 A RESOLUTION
Summary for 1C82
Entry DOI | 10.2210/pdb1c82/pdb |
Descriptor | HYALURONATE LYASE, 4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, CACODYLATE ION, ... (5 entities in total) |
Functional Keywords | protein-carbohydrate complex, lyase |
Biological source | Streptococcus pneumoniae |
Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): Q54873 |
Total number of polymer chains | 1 |
Total formula weight | 84640.53 |
Authors | Ponnuraj, K.,Jedrzejas, M.J. (deposition date: 2000-04-05, release date: 2001-04-05, Last modification date: 2023-12-27) |
Primary citation | Ponnuraj, K.,Jedrzejas, M.J. Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution. J.Mol.Biol., 299:885-895, 2000 Cited by PubMed: 10843845DOI: 10.1006/jmbi.2000.3817 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report