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Calcium in PDB 3dwe: Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline

Enzymatic activity of Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline

All present enzymatic activity of Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline:
3.4.21.64;

Protein crystallography data

The structure of Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline, PDB code: 3dwe was solved by E.Pechkova, S.K.Tripathi, C.Nicolini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.06 / 0.99
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.948, 67.948, 102.388, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 22.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline (pdb code 3dwe). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline, PDB code: 3dwe:

Calcium binding site 1 out of 1 in 3dwe

Go back to Calcium Binding Sites List in 3dwe
Calcium binding site 1 out of 1 in the Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Proteinase K By Classical Hanging Drop Method After High X- Ray Dose on Esrf ID14-2 Beamline within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Ca280

b:0.4
occ:1.00
O X:HOH390 2.4 17.2 1.0
O X:HOH410 2.4 14.0 1.0
O X:PRO175 2.8 6.6 1.0
OD1 X:ASP200 3.0 7.9 1.0
O X:HOH337 3.7 78.0 1.0
O X:HOH399 3.8 21.4 1.0
CG X:ASP200 3.9 5.7 1.0
C X:PRO175 4.0 5.9 1.0
OD2 X:ASP200 4.2 5.5 1.0
O X:VAL177 4.3 5.3 1.0
O X:HOH300 4.6 2.0 1.0
O X:HOH415 4.7 46.1 1.0
O X:HOH389 4.7 14.7 1.0
CA X:PRO175 4.8 6.3 1.0
N X:SER176 4.9 5.5 1.0
CA X:SER176 4.9 5.5 1.0
O X:HOH382 5.0 16.0 1.0

Reference:

E.Pechkova, S.K.Tripathi, C.Nicolini. Radiation Damage in Protein Structural Characterization By Synchrotron Radiation: State of the Art and Nanotechnology-Based Perspective To Be Published.
Page generated: Sat Dec 12 04:09:28 2020

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