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PDBsum entry 3dyb

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Hydrolase PDB id
3dyb
Contents
Protein chain
279 a.a.
Ligands
ADA-ADA
EPE
Metals
_CA ×2
Waters ×379

References listed in PDB file
Key reference
Title High-Resolution structure of proteinase k cocrystallized with digalacturonic acid.
Authors S.B.Larson, J.S.Day, C.Nguyen, R.Cudney, A.Mcpherson.
Ref. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009, 65, 192-198.
PubMed id 19255463
Abstract
Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside the protein, two calcium ions, 379 water molecules, a molecule of DGA and a partially occupied HEPES molecule. The DGA molecule has one sugar moiety disposed exactly on a crystallographic twofold axis; the second ring was not observed. The DGA molecule is bound to two protein molecules across the twofold axis through hydrogen-bonding networks involving Ser150 and water molecules. One of the calcium-ion sites has not been reported previously. This study further illustrates the involvement of small molecules in the crystallization of macromolecules through their ability to form intermolecular lattice interactions.
Secondary reference #1
Title Progress in the development of an alternative approach to macromolecular crystallization
Authors S.B.Larson, J.S.Day, C.Nguyen, R.Cudney, A.Mcpherson.
Ref. CRYST GROWTH DES, 2008, 8, 3038-3052.
PROCHECK
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