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Calcium in PDB 3de6: Proteinase K By Classical Hanging Drop Method After the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline

Enzymatic activity of Proteinase K By Classical Hanging Drop Method After the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline

All present enzymatic activity of Proteinase K By Classical Hanging Drop Method After the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline:
3.4.21.64;

Protein crystallography data

The structure of Proteinase K By Classical Hanging Drop Method After the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline, PDB code: 3de6 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) 35.03 / 2.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.841, 67.841, 102.573, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 23.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Proteinase K By Classical Hanging Drop Method After the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline (pdb code 3de6). 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 the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline, PDB code: 3de6:

Calcium binding site 1 out of 1 in 3de6

Go back to Calcium Binding Sites List in 3de6
Calcium binding site 1 out of 1 in the Proteinase K By Classical Hanging Drop Method After the Third Step of High X-Ray Dose on Esrf ID23-1 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 the Third Step of High X-Ray Dose on Esrf ID23-1 Beamline within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Ca281

b:71.7
occ:1.00
 O X:HOH284 0.4 2.0 1.0
O X:GLU174 2.6 11.8 1.0
O X:VAL177 2.7 16.1 1.0
O X:HOH394 2.7 35.8 1.0
OD2 X:ASP200 3.0 19.6 1.0
O X:HOH321 3.1 24.1 1.0
OG1 X:THR179 3.2 10.8 1.0
O X:VAL198 3.5 16.6 1.0
C X:GLU174 3.6 13.3 1.0
O X:PRO175 3.6 14.6 1.0
CA X:PRO175 3.7 13.4 1.0
C X:PRO175 3.7 14.0 1.0
C X:VAL177 3.7 15.7 1.0
CB X:THR179 3.9 10.7 1.0
CG2 X:VAL198 4.0 23.0 1.0
N X:PRO175 4.0 14.0 1.0
CG X:ASP200 4.0 18.4 1.0
N X:THR179 4.1 12.9 1.0
O X:ALA172 4.2 11.7 1.0
N X:VAL177 4.2 13.4 1.0
CG2 X:VAL177 4.3 12.3 1.0
OD1 X:ASP200 4.3 19.2 1.0
N X:SER176 4.5 13.4 1.0
CA X:VAL177 4.5 14.2 1.0
C X:VAL198 4.6 15.1 1.0
CA X:THR179 4.7 11.9 1.0
N X:CYS178 4.7 16.5 1.0
CA X:GLU174 4.8 13.8 1.0
N X:GLU174 4.8 13.2 1.0
C X:CYS178 4.8 13.2 1.0
CA X:CYS178 4.8 15.9 1.0
O X:HOH374 4.9 28.1 1.0

Reference:

E.Pechkova, S.Tripathi, R.B.Ravelli, S.Mcsweeney, C.Nicolini. Radiation Stability of Proteinase K Crystals Grown By Lb Nanotemplate Method J.Struct.Biol. V. 168 409 2009.
ISSN: ISSN 1047-8477
PubMed: 19686853
DOI: 10.1016/J.JSB.2009.08.005
Page generated: Sat Jul 13 08:59:24 2024

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