3O4P

DFPase at 0.85 Angstrom resolution (H atoms included)

Summary for 3O4P

• Entry DOI: 10.2210/pdb3o4p/pdb
• Related: 1PJX
• Descriptor: Diisopropyl-fluorophosphatase, CALCIUM ION, GLYCEROL, ... (11 entities in total)
• Functional Keywords: beta-propeller, hydrolase
• Biological source: Loligo vulgaris (Common European squid)
• Total number of polymer chains: 1
• Total formula weight: 37265.29

Authors

Liebschner, D.,Elias, M.,Koepke, J.,Lecomte, C.,Guillot, B.,Jelsch, C.,Chabriere, E. (deposition date: 2010-07-27, release date: 2011-08-17, Last modification date: 2024-04-03)

Primary citation

Elias, M.,Liebschner, D.,Koepke, J.,Lecomte, C.,Guillot, B.,Jelsch, C.,Chabriere, E.
Hydrogen atoms in protein structures: high-resolution X-ray diffraction structure of the DFPase.
BMC Res Notes, 6:308-308, 2013

PubMed Abstract: Hydrogen atoms represent about half of the total number of atoms in proteins and are often involved in substrate recognition and catalysis. Unfortunately, X-ray protein crystallography at usual resolution fails to access directly their positioning, mainly because light atoms display weak contributions to diffraction. However, sub-Ångstrom diffraction data, careful modeling and a proper refinement strategy can allow the positioning of a significant part of hydrogen atoms.

PubMed: 23915572
DOI: 10.1186/1756-0500-6-308

Experimental method

X-RAY DIFFRACTION (0.85 Å)