Calcium in PDB 5fxl: Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer

Enzymatic activity of Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer

All present enzymatic activity of Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer:
3.4.21.4;

Protein crystallography data

The structure of Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer, PDB code: 5fxl was solved by M.W.Bowler, D.Nurizzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.49 / 1.78
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.835, 64.682, 69.960, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 21

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer (pdb code 5fxl). 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 Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer, PDB code: 5fxl:

Calcium binding site 1 out of 1 in 5fxl

Go back to Calcium Binding Sites List in 5fxl
Calcium binding site 1 out of 1 in the Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Trypsin Solved By Mr From Data Collected By Direct Data Collection (Ddc) Using the Esrf Robodiff Goniometer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:32.0
occ:1.00
 O A:HOH2032 2.2 33.8 1.0
OE1 A:GLU70 2.3 33.4 1.0
O A:VAL75 2.3 32.2 1.0
O A:ASN72 2.4 31.2 1.0
OE2 A:GLU80 2.4 33.5 1.0
O A:HOH2033 2.4 35.9 1.0
CD A:GLU80 3.3 34.1 1.0
CD A:GLU70 3.3 33.5 1.0
C A:VAL75 3.5 35.5 1.0
C A:ASN72 3.5 31.9 1.0
CG A:GLU80 3.6 33.2 1.0
OE2 A:GLU70 3.7 32.4 1.0
CA A:VAL76 4.2 36.0 1.0
N A:GLU77 4.2 38.2 1.0
N A:VAL76 4.3 36.1 1.0
N A:VAL75 4.3 36.4 1.0
OE1 A:GLU77 4.3 45.4 1.0
O A:HOH2031 4.3 37.2 1.0
CA A:ILE73 4.3 31.6 1.0
N A:ASN72 4.3 33.6 1.0
N A:ILE73 4.4 30.2 1.0
CA A:ASN72 4.4 32.4 1.0
OE1 A:GLU80 4.5 37.2 1.0
CA A:VAL75 4.5 37.2 1.0
C A:ILE73 4.6 33.0 1.0
N A:ASP71 4.7 33.8 1.0
CG A:GLU70 4.7 31.4 1.0
CB A:ASN72 4.7 34.1 1.0
C A:VAL76 4.7 37.6 1.0
CG A:GLU77 4.7 44.3 1.0
CA A:GLU70 4.8 29.9 1.0
CB A:GLU77 4.9 41.7 1.0
N A:ASN74 4.9 35.2 1.0
CD A:GLU77 4.9 45.8 1.0
O A:ILE73 4.9 33.5 1.0
CB A:GLU70 5.0 29.4 1.0

Reference:

D.Nurizzo, M.W.Bowler, H.Caserotto, F.Dobias, T.Giraud, J.Surr, N.Guichard, G.Papp, M.Guijarro, C.Mueller-Dieckmann, D.Flot, S.Mcsweeney, F.Cipriani, P.Theveneau, G.A.Leonard. Robodiff: Combining A Sample Changer and Goniometer For Highly Automated Macromolecular Crystallography Experiments. Acta Crystallogr.,Sect.D V. 72 966 2016.
ISSN: ISSN 0907-4449
PubMed: 27487827
DOI: 10.1107/S205979831601158X
Page generated: Sat Dec 12 05:25:55 2020

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