CHONDROITINASE AC LYASE FROM FLAVOBACTERIUM HEPARINUM
The structure was published by Fethiere, J., Eggimann, B., and Cygler, M., in 1999 in a paper entitled "Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of PROTEIN (CHONDROITINASE AC). This molecule has the UniProt identifier Q59288 (CSLA_PEDHD). The sample contained 678 residues which is 100% of the natural sequence. Out of 678 residues 668 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: