1IEX

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4I,4III,4V-S-trithiocellohexaose

Summary for 1IEX

• Entry DOI: 10.2210/pdb1iex/pdb
• Related: 1EX1 1IEQ 1IEV 1IEW
• Related PRD ID: PRD_900034
• Descriptor: BETA-D-GLUCAN GLUCOHYDROLASE ISOENZYME EXO1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-glucopyranose-(1-4)-4-thio-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: 2-domain fold, hydrolase
• Biological source: Hordeum vulgare
• Total number of polymer chains: 1
• Total formula weight: 67153.20

Authors

Hrmova, M.,DeGori, R.,Fincher, G.B.,Smith, B.J.,Driguez, H.,Varghese, J.N. (deposition date: 2001-04-11, release date: 2001-11-14, Last modification date: 2023-08-16)

Primary citation

Hrmova, M.,Varghese, J.N.,De Gori, R.,Smith, B.J.,Driguez, H.,Fincher, G.B.
Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase.
Structure, 9:1005-1016, 2001

PubMed Abstract: Barley beta-D-glucan glucohydrolases represent family 3 glycoside hydrolases that catalyze the hydrolytic removal of nonreducing glucosyl residues from beta-D-glucans and beta-D-glucooligosaccharides. After hydrolysis is completed, glucose remains bound in the active site.

PubMed: 11709165
DOI: 10.1016/S0969-2126(01)00673-6

Experimental method

X-RAY DIFFRACTION (2.2 Å)