CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES
The structure was published by Clausen, T., Kaiser, J.T., Steegborn, C., Huber, R., and Kessler, D., in 2000 in a paper entitled "Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of L-CYSTEINE/L-CYSTINE C-S LYASE.
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 most likely forms homodimers.
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: