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: 10843845 DOI: 10.1006/jmbi.2000.3817 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation