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

DescriptorHYALURONATE 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 Keywordsprotein-carbohydrate complex, lyase
Biological sourceStreptococcus pneumoniae
Cellular locationSecreted, cell wall; Peptidoglycan-anchor (Potential) Q54873
Total number of polymer chains1
Total molecular weight84640.53
Authors
Ponnuraj, K.,Jedrzejas, M.J. (deposition date: 2000-04-05, release date: 2001-04-05, Last modification date: 2020-07-29)
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
PubMed: 10843845 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.2000.3817
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.7 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.23910 0.1% 6.1% 6.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
167518
PDB entries from 2020-08-12