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Magnesium in PDB 3bdh: Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase

Enzymatic activity of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase

All present enzymatic activity of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase:
3.1.3.1;

Protein crystallography data

The structure of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase, PDB code: 3bdh was solved by J.C.Grigg, M.E.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.449, 103.545, 88.489, 90.00, 105.76, 90.00
R / Rfree (%) 15.2 / 18.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase (pdb code 3bdh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase, PDB code: 3bdh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3bdh

Go back to Magnesium Binding Sites List in 3bdh
Magnesium binding site 1 out of 2 in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:14.6
occ:1.00
O A:HOH1059 2.1 9.8 1.0
O A:HOH1032 2.1 16.0 1.0
OE2 A:GLU322 2.1 9.8 1.0
OG1 A:THR155 2.1 8.7 1.0
O A:HOH1056 2.2 11.5 1.0
O A:HOH520 2.2 14.4 1.0
CD A:GLU322 3.1 10.4 1.0
CB A:THR155 3.1 7.3 1.0
OE1 A:GLU322 3.4 9.4 1.0
OD2 A:ASP153 3.7 13.1 1.0
N A:THR155 4.0 7.8 1.0
OD2 A:ASP51 4.1 17.3 1.0
CG2 A:THR155 4.2 8.2 1.0
CA A:THR155 4.2 8.1 1.0
O A:HOH502 4.2 10.0 1.0
CB A:SER102 4.4 9.7 1.0
OD2 A:ASP369 4.4 12.2 1.0
OG A:SER102 4.4 18.2 1.0
CG A:GLU322 4.4 9.1 1.0
CG A:ASP51 4.5 14.8 1.0
O A:HOH1012 4.5 38.2 1.0
CB A:ASP51 4.6 11.8 1.0
CG A:ASP153 4.6 11.5 1.0
O A:HOH1014 4.7 20.0 1.0
CB A:ALA324 4.8 14.9 1.0
CD A:PRO156 4.9 9.1 1.0
O A:HOH1057 5.0 22.9 1.0

Magnesium binding site 2 out of 2 in 3bdh

Go back to Magnesium Binding Sites List in 3bdh
Magnesium binding site 2 out of 2 in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg500

b:13.5
occ:1.00
O B:HOH1070 2.1 11.7 1.0
O B:HOH1065 2.1 12.1 1.0
OE2 B:GLU322 2.1 10.0 1.0
O B:HOH1056 2.1 10.1 1.0
O B:HOH508 2.1 8.5 1.0
OG1 B:THR155 2.2 9.5 1.0
CD B:GLU322 3.1 10.4 1.0
CB B:THR155 3.2 7.6 1.0
OE1 B:GLU322 3.5 10.2 1.0
OD2 B:ASP153 3.6 13.9 1.0
N B:THR155 4.0 8.2 1.0
OD2 B:ASP51 4.1 17.5 1.0
O B:HOH505 4.2 8.4 1.0
CA B:THR155 4.2 8.3 1.0
CG2 B:THR155 4.2 8.7 1.0
OD2 B:ASP369 4.3 11.7 1.0
OG B:SER102 4.4 19.1 1.0
CG B:GLU322 4.4 10.2 1.0
CB B:SER102 4.4 9.6 1.0
CG B:ASP51 4.4 13.8 1.0
CB B:ASP51 4.6 10.6 1.0
CG B:ASP153 4.6 12.8 1.0
O B:HOH1032 4.6 22.2 1.0
CB B:ALA324 4.7 11.0 1.0
CD B:PRO156 5.0 8.4 1.0

Reference:

J.C.Grigg, C.Hucaluk, M.E.Murphy, H.Ritter, J.Yee, S.Rafferty. The Active-Site Trimetallic Cluster of Alkaline Phosphatase Is Lost Upon Isosteric Mutation at the MG2+-Coordinating Residue Threonine-155 To Be Published.
Page generated: Wed Aug 14 09:09:23 2024

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