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Magnesium in PDB 2i34: The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound

Enzymatic activity of The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound

All present enzymatic activity of The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound:
3.1.3.2;

Protein crystallography data

The structure of The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound, PDB code: 2i34 was solved by R.L.Felts, J.J.Tanner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.23 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.000, 89.940, 104.120, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 22.4

Other elements in 2i34:

The structure of The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound also contains other interesting chemical elements:

Tungsten (W) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound (pdb code 2i34). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound, PDB code: 2i34:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2i34

Go back to Magnesium Binding Sites List in 2i34
Magnesium binding site 1 out of 2 in the The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:11.5
occ:1.00
O2 A:WO4401 1.8 18.7 0.8
OD2 A:ASP65 2.0 25.3 1.0
OD1 A:ASP180 2.1 23.3 1.0
O A:HOH441 2.1 18.7 1.0
O A:ASP67 2.1 24.1 1.0
O A:HOH452 2.1 18.1 1.0
CG A:ASP65 3.0 24.4 1.0
CG A:ASP180 3.0 24.6 1.0
OD2 A:ASP180 3.3 26.0 1.0
C A:ASP67 3.3 24.7 1.0
OD1 A:ASP65 3.3 24.5 1.0
W A:WO4401 3.7 21.1 0.8
O A:HOH405 3.8 18.6 1.0
OD2 A:ASP184 4.0 22.5 1.0
CA A:ASP67 4.1 25.0 1.0
OG1 A:THR69 4.1 25.0 1.0
N A:ASP67 4.1 25.1 1.0
CB A:ASP65 4.2 24.6 1.0
CB A:ASP67 4.3 25.4 1.0
OH A:TYR219 4.3 25.1 1.0
O A:HOH453 4.3 20.1 1.0
N A:GLU68 4.4 24.7 1.0
CB A:GLU68 4.4 24.4 1.0
CB A:ASP180 4.4 24.4 1.0
CA A:GLU68 4.6 24.6 1.0
C A:GLU68 4.6 24.2 1.0
N A:ASP180 4.7 24.2 1.0
N A:THR69 4.7 24.1 1.0
O3 A:WO4401 4.7 14.8 0.8
O4 A:WO4401 4.8 15.7 0.8
OD1 A:ASP184 4.8 22.2 1.0
CG A:ASP184 4.8 23.0 1.0
C A:LEU66 4.8 24.6 1.0
CB A:ASN181 4.9 24.3 1.0
O1 A:WO4401 5.0 18.5 0.8

Magnesium binding site 2 out of 2 in 2i34

Go back to Magnesium Binding Sites List in 2i34
Magnesium binding site 2 out of 2 in the The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of Class C Acid Phosphatase From Bacillus Anthracis with Tungstate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg302

b:11.5
occ:1.00
O1 B:WO4402 1.8 22.2 0.8
O B:HOH418 2.0 18.2 1.0
OD2 B:ASP65 2.1 26.8 1.0
O B:HOH420 2.1 12.6 1.0
O B:ASP67 2.1 24.1 1.0
OD1 B:ASP180 2.1 26.1 1.0
CG B:ASP65 3.0 24.8 1.0
CG B:ASP180 3.1 26.6 1.0
C B:ASP67 3.3 24.2 1.0
OD1 B:ASP65 3.4 22.0 1.0
OD2 B:ASP180 3.4 26.8 1.0
W B:WO4402 3.6 26.6 0.8
O B:HOH417 3.8 18.2 1.0
CA B:ASP67 4.0 24.2 1.0
OD2 B:ASP184 4.0 23.7 1.0
OG1 B:THR69 4.1 22.7 1.0
N B:ASP67 4.2 24.2 1.0
CB B:ASP67 4.2 24.8 1.0
O B:HOH500 4.3 19.0 1.0
CB B:ASP65 4.3 24.8 1.0
OH B:TYR219 4.3 26.6 1.0
N B:GLU68 4.4 23.4 1.0
CB B:ASP180 4.5 25.4 1.0
CB B:GLU68 4.5 23.8 1.0
O2 B:WO4402 4.6 22.9 0.8
O3 B:WO4402 4.6 23.2 0.8
N B:ASP180 4.7 24.9 1.0
CA B:GLU68 4.7 23.8 1.0
C B:GLU68 4.7 23.4 1.0
OD1 B:ASP184 4.9 24.6 1.0
CB B:ASN181 4.9 25.4 1.0
CG B:ASP184 4.9 24.7 1.0
N B:THR69 4.9 23.5 1.0
C B:LEU66 4.9 23.9 1.0
O4 B:WO4402 5.0 23.1 0.8

Reference:

R.L.Felts, J.J.Tanner. The Crystal Structure of the Class C Acid Phosphatase From Bacillus Anthracis To Be Published.
Page generated: Mon Dec 14 07:26:49 2020

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