CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE
The structure was published by Van Roey, P., Rao, V., Plummer Jr., T.H., and Tarentino, A.L., in 1994 in a paper entitled "Crystal structure of endo-beta-N-acetylglucosaminidase F1, an alpha/beta-barrel enzyme adapted for a complex substrate." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1. This molecule has the UniProt identifier P36911 (EBA1_ELIME). The sample contained 289 residues which is 100% of the natural sequence. Out of 289 residues 285 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: