CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS
The structure was published by Lauble, H., Forster, S., Miehlich, B., Wajant, H., and Effenberger, F., in 2001 in a paper entitled "Structure of Hydroxynitrile Lyase from Manihot Esculenta in Complex with Substrates Acetone and Chloroacetone: Implications for the Mechanism of Cyanogenesis" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of HYDROXYNITRILE 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: