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Calcium in PDB 7obs: Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide

Enzymatic activity of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide

All present enzymatic activity of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide:
2.7.10.2; 2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide, PDB code: 7obs was solved by F.Centorrino, B.Andlovic, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.36 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.612, 111.816, 62.713, 90, 90, 90
R / Rfree (%) 14.6 / 18.9

Other elements in 7obs:

The structure of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide (pdb code 7obs). 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 Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide, PDB code: 7obs:

Calcium binding site 1 out of 1 in 7obs

Go back to Calcium Binding Sites List in 7obs
Calcium binding site 1 out of 1 in the Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of 14-3-3 Sigma in Complex with RIPK2 Phosphopeptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:9.3
occ:1.00
 O A:GLU110 2.3 8.2 1.0
O A:HOH661 2.3 11.2 1.0
O A:HOH520 2.3 14.0 1.0
OE2 A:GLU35 2.5 9.2 1.0
OE1 A:GLU35 2.6 14.3 1.0
CD A:GLU35 2.9 19.2 1.0
C A:GLU110 3.5 7.7 1.0
H A:GLY112 3.5 8.8 1.0
HB3 A:GLU110 3.8 11.9 0.4
HA A:ALA111 3.9 7.0 1.0
HB3 A:GLU110 3.9 12.0 0.6
N A:GLY112 4.1 7.3 1.0
O A:HOH671 4.1 25.5 1.0
HA A:GLU110 4.3 8.0 0.6
HA A:GLU110 4.3 8.1 0.4
CG A:GLU35 4.3 8.2 1.0
HA3 A:GLY112 4.4 12.8 1.0
CA A:GLU110 4.4 6.8 0.4
CA A:GLU110 4.4 6.7 0.6
N A:ALA111 4.4 5.8 1.0
CA A:ALA111 4.5 5.8 1.0
O A:HOH584 4.5 14.6 1.0
CB A:GLU110 4.5 10.0 0.4
OE1 A:GLU110 4.5 8.2 0.4
HG2 A:GLU35 4.5 9.9 1.0
CB A:GLU110 4.6 10.0 0.6
O A:HOH507 4.6 26.6 1.0
C A:ALA111 4.7 8.8 1.0
O A:HOH552 4.7 12.6 1.0
HG3 A:GLU35 4.8 9.9 1.0
CA A:GLY112 4.8 10.7 1.0
O A:HOH678 4.9 27.2 1.0
HB2 A:GLU110 5.0 12.0 0.6

Reference:

B.Andlovic, G.Heilmann, S.Ninck, S.Andrei, F.Centorrino, Y.Higuchi, N.Kato, L.Brunsveld, S.Menninger, A.Choidas, A.Wolf, M.Kaiser, J.Eickhoff, C.Ottmann. Inf Alpha Primes Ovarian Cancer Cells For Fusicoccin-Induced Cell Death Via Stabilization of 14-3-3 Protein-Protein Interactions To Be Published.
Page generated: Fri Jul 19 02:29:25 2024

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