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). 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):
This entry contains 1 unique UniProt protein: