CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION
The structure was published by Vallee, F., Lipari, F., Yip, P., Sleno, B., Herscovics, A., and Howell, P.L., in 2000 in a paper entitled "Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.54 Å and deposited in 1999.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of CLASS I ALPHA-1,2-MANNOSIDASE. This molecule has the UniProt identifier P32906 (MNS1_YEAST). The sample contained 511 residues which is 93% of the natural sequence. Out of 511 residues 508 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: