GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE
The structure was published by Aleshin, A.E., Stoffer, B., Firsov, L.M., Svensson, B., and Honzatko, R.B., in 1996 in a paper entitled "Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1996.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of GLUCOAMYLASE-471. This molecule has the UniProt identifier P69327 (AMYG_ASPAW). The sample contained 471 residues which is < 90% of the natural sequence. Out of 471 residues 471 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: