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Magnesium in PDB 1n9k: Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution

Enzymatic activity of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution

All present enzymatic activity of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution:
3.1.3.2;

Protein crystallography data

The structure of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution, PDB code: 1n9k was solved by V.Calderone, C.Forleo, M.Benvenuti, G.M.Rossolini, M.C.Thaller, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.32 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 49.499, 92.616, 138.247, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.1

Other elements in 1n9k:

The structure of Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution also contains other interesting chemical elements:

Bromine (Br) 15 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution (pdb code 1n9k). 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 the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution, PDB code: 1n9k:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1n9k

Go back to Magnesium Binding Sites List in 1n9k
Magnesium binding site 1 out of 2 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


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 the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1213

b:7.6
occ:1.00
 OD1 A:ASP167 1.9 12.1 1.0
O A:HOH1277 2.0 15.5 1.0
O A:HOH1296 2.0 10.0 1.0
O A:HOH1395 2.0 16.9 1.0
OD2 A:ASP44 2.1 14.8 1.0
O A:ASP46 2.1 9.8 1.0
CG A:ASP167 3.0 14.8 1.0
CG A:ASP44 3.1 20.5 1.0
C A:ASP46 3.3 13.4 1.0
OD2 A:ASP167 3.4 12.9 1.0
OD1 A:ASP44 3.4 18.7 1.0
OG1 A:THR48 3.9 12.2 1.0
OG A:SER168 3.9 22.1 1.0
N A:ASP46 3.9 13.4 1.0
OD2 A:ASP171 4.0 19.0 1.0
O A:HOH1297 4.0 26.4 1.0
CA A:ASP46 4.0 12.7 1.0
O A:HOH1230 4.1 13.1 1.0
CB A:ASP46 4.2 13.8 1.0
O A:HOH1262 4.4 17.2 1.0
CB A:ASP167 4.4 12.8 1.0
N A:ASP47 4.4 14.4 1.0
CB A:ASP44 4.4 14.8 1.0
N A:ASP167 4.5 14.9 1.0
CB A:ASP47 4.5 13.9 1.0
N A:THR48 4.6 14.5 1.0
N A:SER168 4.7 16.4 1.0
CA A:ASP47 4.7 14.4 1.0
C A:ASP47 4.7 15.4 1.0
CB A:SER168 4.8 19.0 1.0
C A:ILE45 4.8 13.8 1.0
CB A:THR48 4.8 14.7 1.0
O A:HOH1226 4.8 16.2 1.0
CA A:ASP167 4.9 14.8 1.0
O A:HOH1218 5.0 13.6 1.0

Magnesium binding site 2 out of 2 in 1n9k

Go back to Magnesium Binding Sites List in 1n9k
Magnesium binding site 2 out of 2 in the Crystal Structure of the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution


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 the Bromide Adduct of Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli at 2.2 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1214

b:13.8
occ:1.00
 OD2 B:ASP44 2.0 20.3 1.0
O B:HOH1380 2.0 10.3 1.0
O B:HOH1293 2.0 15.7 1.0
OD1 B:ASP167 2.1 16.6 1.0
O B:ASP46 2.1 12.7 1.0
CG B:ASP44 3.0 23.3 1.0
CG B:ASP167 3.1 15.4 1.0
C B:ASP46 3.3 15.4 1.0
OD2 B:ASP167 3.4 16.7 1.0
OD1 B:ASP44 3.4 18.5 1.0
O B:HOH1347 3.8 31.8 1.0
OG1 B:THR48 3.9 15.0 1.0
N B:ASP46 4.0 12.8 1.0
OG B:SER168 4.0 19.1 1.0
CA B:ASP46 4.0 14.4 1.0
OD2 B:ASP171 4.1 23.2 1.0
CB B:ASP46 4.1 14.0 1.0
O B:HOH1230 4.2 16.1 1.0
N B:ASP47 4.4 16.5 1.0
CB B:ASP44 4.4 17.5 1.0
CB B:ASP47 4.4 14.3 1.0
O B:HOH1253 4.5 18.6 1.0
CB B:ASP167 4.5 16.3 1.0
N B:THR48 4.6 15.5 1.0
N B:ASP167 4.6 16.9 1.0
CA B:ASP47 4.7 14.7 1.0
C B:ASP47 4.7 14.9 1.0
C B:ILE45 4.8 14.3 1.0
N B:SER168 4.8 17.2 1.0
O B:HOH1220 4.8 20.6 1.0
CB B:THR48 4.9 13.7 1.0
CB B:SER168 4.9 18.7 1.0

Reference:

V.Calderone, C.Forleo, M.Benvenuti, M.C.Thaller, G.M.Rossolini, S.Mangani. The First Structure of A Bacterial Class B Acid Phosphatase Reveals Further Structural Heterogeneity Among Phosphatases of the Haloacid Dehalogenase Fold. J.Mol.Biol. V. 335 761 2004.
ISSN: ISSN 0022-2836
PubMed: 14687572
DOI: 10.1016/J.JMB.2003.10.050
Page generated: Tue Aug 13 09:47:03 2024

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