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Magnesium in PDB 3u7e: Crystal Structure of Mpnkp Catalytic Fragment (D170A)

Enzymatic activity of Crystal Structure of Mpnkp Catalytic Fragment (D170A)

All present enzymatic activity of Crystal Structure of Mpnkp Catalytic Fragment (D170A):
2.7.1.78; 3.1.3.32;

Protein crystallography data

The structure of Crystal Structure of Mpnkp Catalytic Fragment (D170A), PDB code: 3u7e was solved by N.Coquelle, Z.Havali, N.Bernstein, R.Green, J.N.M.Glover, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.30 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.820, 63.190, 68.120, 90.00, 88.23, 90.00
R / Rfree (%) 16.1 / 19.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mpnkp Catalytic Fragment (D170A) (pdb code 3u7e). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Mpnkp Catalytic Fragment (D170A), PDB code: 3u7e:

Magnesium binding site 1 out of 1 in 3u7e

Go back to Magnesium Binding Sites List in 3u7e
Magnesium binding site 1 out of 1 in the Crystal Structure of Mpnkp Catalytic Fragment (D170A)


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 Mpnkp Catalytic Fragment (D170A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg523

b:50.2
occ:0.73
O B:HOH834 2.0 27.0 1.0
O3 B:PO41 2.1 22.8 1.0
O B:ASP172 2.1 18.8 1.0
OD1 B:ASP288 2.2 23.7 1.0
O B:HOH835 2.9 36.0 1.0
CG B:ASP288 3.1 25.1 1.0
C B:ASP172 3.3 14.4 1.0
OD2 B:ASP288 3.4 29.5 1.0
HB2 B:ASP172 3.5 22.3 1.0
HG1 B:THR174 3.5 17.3 1.0
HB1 B:ALA170 3.5 13.2 1.0
P B:PO41 3.6 17.4 1.0
O B:HOH693 3.8 36.3 1.0
H B:ASP288 3.9 13.3 1.0
HA3 B:GLY173 4.0 14.1 1.0
HE2 B:PHE305 4.0 51.6 1.0
HB3 B:ALA170 4.0 13.2 1.0
H B:ASP172 4.0 14.8 1.0
HZ B:PHE305 4.1 47.9 1.0
OD2 B:ASP309 4.1 11.8 1.0
CA B:ASP172 4.1 13.8 1.0
O4 B:PO41 4.1 12.0 1.0
N B:ASP172 4.2 12.4 1.0
CB B:ASP172 4.2 18.6 1.0
H B:ALA289 4.2 15.2 1.0
CB B:ALA170 4.2 11.0 1.0
OG1 B:THR174 4.2 14.5 1.0
N B:GLY173 4.3 11.5 1.0
HB2 B:ALA289 4.3 16.1 1.0
O B:HOH103 4.4 26.4 1.0
O1 B:PO41 4.4 13.6 1.0
O2 B:PO41 4.4 22.0 1.0
HB3 B:ASP172 4.5 22.3 1.0
CB B:ASP288 4.5 18.8 1.0
CA B:GLY173 4.5 11.8 1.0
HB2 B:ALA170 4.6 13.2 1.0
H B:LEU171 4.6 11.3 1.0
CE2 B:PHE305 4.7 43.1 1.0
N B:ASP288 4.7 11.1 1.0
N B:ALA289 4.7 12.7 1.0
CZ B:PHE305 4.7 40.0 1.0
HB3 B:ASP288 4.8 22.5 1.0
C B:GLY173 4.8 13.3 1.0
HZ1 B:LYS259 4.8 11.9 1.0
HB B:THR174 4.9 14.6 1.0
H B:THR174 4.9 14.3 1.0
C B:LEU171 4.9 9.9 1.0
N B:THR174 5.0 12.0 1.0

Reference:

N.Coquelle, Z.Havali-Shahriari, N.Bernstein, R.Green, J.N.Glover. Structural Basis For the Phosphatase Activity of Polynucleotide Kinase/Phosphatase on Single- and Double-Stranded Dna Substrates. Proc.Natl.Acad.Sci.Usa V. 108 21022 2011.
ISSN: ISSN 0027-8424
PubMed: 22171004
DOI: 10.1073/PNAS.1112036108
Page generated: Thu Aug 15 12:24:20 2024

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