CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI
The structure was published by Clausen, T., Huber, R., Laber, B., Pohlenz, H.D., and Messerschmidt, A., in 1996 in a paper entitled "Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.83 Å and deposited in 1997.
The experimental data on which the structure is based was not deposited.
This PDB entry contains multiple copies of the structure of CYSTATHIONINE BETA-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 homotetramers.
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: