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4D4A

Structure of the catalytic domain (BcGH76) of the Bacillus circulans GH76 alpha mannanase, Aman6.

Summary for 4D4A
Entry DOI10.2210/pdb4d4a/pdb
Related4D4B 4D4C 4D4D 5AGD
DescriptorALPHA-1,6-MANNANASE, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordshydrolase, glycoside hydrolase, gh76, cazy, mannan, enzyme-carbohydrate interaction, glycosidase inhibition, quantum mechanics, transition state
Biological sourceBACILLUS CIRCULANS
Total number of polymer chains2
Total formula weight82296.19
Authors
Thompson, A.J.,Speciale, G.,Iglesias-Fernandez, J.,Hakki, Z.,Belz, T.,Cartmell, A.,Spears, R.J.,Stepper, J.,Gilbert, H.J.,Rovira, C.,Williams, S.J.,Davies, G.J. (deposition date: 2014-10-27, release date: 2015-03-25, Last modification date: 2023-12-20)
Primary citationThompson, A.J.,Speciale, G.,Iglesias-Fernandez, J.,Hakki, Z.,Belz, T.,Cartmell, A.,Spears, R.J.,Chandler, E.,Temple, M.J.,Stepper, J.,Gilbert, H.J.,Rovira, C.,Williams, S.J.,Davies, G.J.
Evidence for a Boat Conformation at the Transition State of Gh76 Alpha-1,6-Mannanases- Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism
Angew.Chem.Int.Ed.Engl., 54:5378-, 2015
Cited by
PubMed: 25772148
DOI: 10.1002/ANIE.201410502
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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