MYROSINASE FROM SINAPIS ALBA
The structure was published by Burmeister, W.P., Cottaz, S., Rollin, P., Vasella, A., and Henrissat, B., in 2000 in a paper entitled "High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of MYROSINASE MA1. This molecule has the UniProt identifier P29736 (MYRA_SINAL). The sample contained 501 residues which is 100% of the natural sequence. Out of 501 residues 499 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 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: