5ptp

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5ptp, resolution 1.34Å

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STRUCTURE OF HYDROLASE (SERINE PROTEINASE)

Overview

The solvent structure in orthorhombic crystals of bovine trypsin has been, independently determined by X-ray diffraction to 1.35 A resolution and by, neutron diffraction to 2.1 A resolution. A consensus model of the water, molecule positions was obtained using oxygen positions identified in the, electron density map determined by X-ray diffraction, which were verified, by comparison to D2O-H2O difference neutron scattering density. Six of 184, water molecules in the X-ray structure, all with B-factors greater than 50, A2, were found to be spurious after comparison with neutron results., Roughly two-thirds of the water of hydration expected from thermodynamic, data for proteins was localized by neutron diffraction; approximately, one-half of the water of hydration was located by X-ray ... [(full description)]

About this Structure

5PTP is a [Single protein] structure of sequence from [Bos taurus] with CA as [ligand]. This structure superseeds the now removed PDB entries 4PTP, 3PTP, 2PTP and 1PTP. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Sites: BIN, CAT and ION. Full crystallographic information is available from [OCA].

Reference

Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction., Finer-Moore JS, Kossiakoff AA, Hurley JH, Earnest T, Stroud RM, Proteins. 1992 Mar;12(3):203-22. PMID:1557349

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