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Calcium in PDB 1ywt: Crystal Structure of the Human Sigma Isoform of 14-3-3 in Complex with A Mode-1 Phosphopeptide

Protein crystallography data

The structure of Crystal Structure of the Human Sigma Isoform of 14-3-3 in Complex with A Mode-1 Phosphopeptide, PDB code: 1ywt was solved by E.W.Wilker, R.A.Grant, S.C.Artim, M.B.Yaffe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.68 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 56.173, 137.093, 155.313, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 28.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Human Sigma Isoform of 14-3-3 in Complex with A Mode-1 Phosphopeptide (pdb code 1ywt). 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 the Human Sigma Isoform of 14-3-3 in Complex with A Mode-1 Phosphopeptide, PDB code: 1ywt:

Calcium binding site 1 out of 1 in 1ywt

Go back to Calcium Binding Sites List in 1ywt
Calcium binding site 1 out of 1 in the Crystal Structure of the Human Sigma Isoform of 14-3-3 in Complex with A Mode-1 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 the Human Sigma Isoform of 14-3-3 in Complex with A Mode-1 Phosphopeptide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca249

b:46.2
occ:0.50
O B:HOH279 1.9 20.5 1.0
NE2 B:HIS106 2.0 59.4 1.0
CE1 B:HIS106 2.9 58.1 1.0
CD2 B:HIS106 3.1 57.0 1.0
OE2 B:GLU31 3.4 70.8 1.0
CG B:GLU31 3.9 64.8 1.0
CD B:GLU31 3.9 68.9 1.0
ND1 B:HIS106 4.0 57.4 1.0
CG B:HIS106 4.1 56.2 1.0
CB B:GLU31 4.3 60.9 1.0
OG B:SER105 4.7 52.5 1.0
CA B:GLU31 4.8 58.3 1.0
OE1 B:GLU31 5.0 70.3 1.0

Reference:

E.W.Wilker, R.A.Grant, S.C.Artim, M.B.Yaffe. A Structural Basis For 14-3-3SIGMA Functional Specificity. J.Biol.Chem. V. 280 18891 2005.
ISSN: ISSN 0021-9258
PubMed: 15731107
DOI: 10.1074/JBC.M500982200
Page generated: Sat Dec 12 03:29:28 2020

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