Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4I,4III,4V-S-trithiocellohexaose
The structure was published by Hrmova, M., Varghese, J.N., De Gori, R., Smith, B.J., Driguez, H., and Fincher, G.B., in 2001 in a paper entitled "Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2001.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of BETA-D-GLUCAN GLUCOHYDROLASE ISOENZYME EXO1.
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: