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Calcium in PDB 5n6n: Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex

Enzymatic activity of Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex

All present enzymatic activity of Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex:
3.2.1.28;

Protein crystallography data

The structure of Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex, PDB code: 5n6n was solved by M.Alblova, A.Smidova, V.Obsilova, T.Obsil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.16 / 2.29
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 160.805, 104.749, 105.638, 90.00, 121.89, 90.00
R / Rfree (%) 18.4 / 23.7

Other elements in 5n6n:

The structure of Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex also contains other interesting chemical elements:

Arsenic (As) 5 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex (pdb code 5n6n). 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 14-3-3:Neutral Trehalase NTH1 Complex, PDB code: 5n6n:

Calcium binding site 1 out of 1 in 5n6n

Go back to Calcium Binding Sites List in 5n6n
Calcium binding site 1 out of 1 in the Crystal Structure of the 14-3-3:Neutral Trehalase NTH1 Complex


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 14-3-3:Neutral Trehalase NTH1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca801

b:30.1
occ:1.00
OD1 C:ASP114 2.2 32.3 1.0
OD2 C:ASP125 2.3 25.1 1.0
OD1 C:ASP116 2.3 37.0 1.0
O C:GLN120 2.3 34.8 1.0
OD1 C:ASN118 2.4 29.7 1.0
O C:HOH961 2.5 28.9 1.0
OD1 C:ASP125 2.6 28.1 1.0
CG C:ASP125 2.7 28.5 1.0
CG C:ASP116 3.2 34.9 1.0
CG C:ASN118 3.2 31.4 1.0
C C:GLN120 3.4 30.1 1.0
CG C:ASP114 3.4 30.2 1.0
OD2 C:ASP116 3.4 32.6 1.0
ND2 C:ASN118 3.6 27.6 1.0
CA C:ASP114 4.0 31.1 1.0
N C:GLN120 4.1 29.6 1.0
CA C:GLN120 4.1 33.4 1.0
CB C:ASP114 4.1 30.4 1.0
CB C:ASP125 4.3 24.1 1.0
N C:ASN118 4.3 30.9 1.0
CB C:GLN120 4.3 25.6 1.0
OD2 C:ASP114 4.3 32.4 1.0
N C:ILE121 4.3 28.4 1.0
N C:ASP116 4.4 34.0 1.0
CA C:ILE121 4.5 29.5 1.0
C C:ASP114 4.5 29.2 1.0
CB C:ASN118 4.5 26.0 1.0
N C:THR115 4.5 29.1 1.0
CB C:ASP116 4.5 32.8 1.0
N C:LYS117 4.6 33.9 1.0
N C:THR122 4.6 24.0 1.0
OG1 C:THR122 4.8 27.6 1.0
CA C:ASN118 4.8 33.1 1.0
CA C:ASP116 4.8 30.8 1.0
C C:ASP116 4.9 35.1 1.0
C C:ASN118 5.0 32.8 1.0

Reference:

M.Alblova, A.Smidova, V.Docekal, J.Vesely, P.Herman, V.Obsilova, T.Obsil. Molecular Basis of the 14-3-3 Protein-Dependent Activation of Yeast Neutral Trehalase NTH1. Proc. Natl. Acad. Sci. V. 114 E9811 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29087344
DOI: 10.1073/PNAS.1714491114
Page generated: Mon Jul 15 08:50:05 2024

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