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Calcium in PDB 8jnx: Alkaline Amylase AMY703 with Truncated of N-Terminus Domain

Protein crystallography data

The structure of Alkaline Amylase AMY703 with Truncated of N-Terminus Domain, PDB code: 8jnx was solved by L.Xiang, G.Zhang, J.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.46 / 3.20
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 171.307, 171.307, 167.17, 90, 90, 120
R / Rfree (%) 20.7 / 24.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Alkaline Amylase AMY703 with Truncated of N-Terminus Domain (pdb code 8jnx). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Alkaline Amylase AMY703 with Truncated of N-Terminus Domain, PDB code: 8jnx:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 8jnx

Go back to Calcium Binding Sites List in 8jnx
Calcium binding site 1 out of 2 in the Alkaline Amylase AMY703 with Truncated of N-Terminus Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Alkaline Amylase AMY703 with Truncated of N-Terminus Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca701

b:78.3
occ:1.00
OD1 A:ASP321 3.2 60.3 1.0
OD2 A:ASP321 3.6 55.4 1.0
CG A:ASP321 3.8 55.6 1.0
CD2 A:TYR206 4.3 49.6 1.0
CZ2 A:TRP352 4.4 74.8 1.0
CZ A:PHE281 4.6 56.6 1.0
CG A:TYR206 4.6 50.0 1.0
CH2 A:TRP352 4.6 79.2 1.0
CE2 A:PHE281 4.8 50.1 1.0
CE2 A:TYR206 4.8 48.6 1.0
CB A:TYR206 4.8 53.6 1.0
OE1 A:GLU350 5.0 57.7 1.0

Calcium binding site 2 out of 2 in 8jnx

Go back to Calcium Binding Sites List in 8jnx
Calcium binding site 2 out of 2 in the Alkaline Amylase AMY703 with Truncated of N-Terminus Domain


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Alkaline Amylase AMY703 with Truncated of N-Terminus Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca702

b:89.8
occ:1.00
O A:ASP465 3.4 135.4 1.0
OD2 A:ASP468 3.8 54.3 1.0
OD1 A:ASP465 3.9 152.3 1.0
OD1 A:ASP468 4.1 65.4 1.0
C A:ASP465 4.2 138.9 1.0
CD2 A:TRP466 4.3 96.6 1.0
CE2 A:TRP466 4.4 98.3 1.0
CE3 A:TRP466 4.4 89.1 1.0
CG A:ASP468 4.4 56.7 1.0
CZ3 A:TRP466 4.5 82.1 1.0
CZ2 A:TRP466 4.6 95.0 1.0
CG A:ASP465 4.6 152.9 1.0
CH2 A:TRP466 4.6 87.4 1.0
CG A:TRP466 4.8 96.8 1.0
CA A:TRP466 4.8 96.3 1.0
N A:TRP466 4.9 118.4 1.0
NE1 A:TRP466 4.9 99.5 1.0

Reference:

L.Xiang, G.Zhang, J.Zhou. Truncation of N-Terminus Domain of Alkaline A-Amylase to Form A Unique Dimer Leads to Improved Activity and Stability and Decreased Calcium Ion Dependence To Be Published.
Page generated: Thu Jul 10 05:32:03 2025

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