1c82 Summary

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MECHANISM OF HYALURONAN BINDING AND DEGRADATION: STRUCTURE OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE IN COMPLEX WITH HYALURONIC ACID DISACCHARIDE AT 1.7 A RESOLUTION

The structure was published by Ponnuraj, K. and Jedrzejas, M.J., in 2000 in a paper entitled "Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2000.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of HYALURONATE LYASE. This molecule has the UniProt identifier Q54873 (HYSA_STRPN)search. The sample contained 731 residues which is < 90% of the natural sequence. Out of 731 residues 718 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A HYALURONATE LYASE Q54873 (285-1009) (HYSA_STRPN)search Streptococcus pneumoniae TIGR4search < 90% 731 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q54873 (285 - 1009) HYALURONATE LYASE Streptococcus pneumoniae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Hyaluronate lyase-like catalytic, N-terminal domainsearch, Hyaluronate lyase-like, C-terminal domainsearch, Hyaluronate lyase-like, central domainsearch Beta-galactosidase; Chain A, domain 5search, Glycosyltransferasesearch, Chondroitinase Ac; Chain A, domain 3search Polysaccharide lyase family 8, super-sandwich domainsearch, Polysaccharide lyase family 8, C-terminal beta-sandwich domainsearch, Polysaccharide lyase family 8, N terminal alpha-helical domainsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A (Q54873) extracellular regionsearch carbon-oxygen lyase activity, acting on polysaccharidessearch catalytic activitysearch lyase activitysearch carbohydrate bindingsearch carbohydrate metabolic processsearch

Chain InterPro annotation
A Polysaccharide lyase family 8, central domainsearch Polysaccharide lyase family 8, C-terminalsearch Chondroitin AC/alginate lyasesearch Galactose mutarotase-like domainsearch Polysaccharide lyase family 8-like, C-terminalsearch Polysaccharide lyase family 8, N-terminalsearch Polysaccharide lyase 8, N-terminal alpha-helicalsearch Glycoside hydrolase-type carbohydrate-binding, subgroupsearch