CELLULOMONAS FIMI XYLANASE/CELLULASE DOUBLE MUTANT E127A/H205N WITH COVALENT CELLOBIOSE
The structure was published by Notenboom, V., Birsan, C., Nitz, M., Rose, D.R., Warren, R.A., and Withers, S.G., in 1998 in a paper entitled "Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.84 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of CELLULOMONAS FIMI FAMILY 10 BETA-1,4-GLYCANASE. This molecule has the UniProt identifier P07986 (GUX_CELFI). The sample contained 312 residues which is < 90% of the natural sequence. Out of 312 residues 311 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: