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Magnesium in PDB 1q92: Crystal Structure of Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U

Enzymatic activity of Crystal Structure of Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U

All present enzymatic activity of Crystal Structure of Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U:
3.1.3.5;

Protein crystallography data

The structure of Crystal Structure of Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U, PDB code: 1q92 was solved by A.Rinaldo-Matthis, C.Rampazzo, J.Balzarini, P.Reichard, V.Bianchi, P.Nordlund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.32 / 1.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.758, 73.758, 105.981, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 16.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U (pdb code 1q92). 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 Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U, PDB code: 1q92:

Magnesium binding site 1 out of 1 in 1q92

Go back to Magnesium Binding Sites List in 1q92
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U


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 Human Mitochondrial Deoxyribonucleotidase in Complex with the Inhibitor Pmcp-U within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1003

b:14.2
occ:1.00
OD2 A:ASP41 2.0 15.8 1.0
O A:HOH2135 2.1 17.5 1.0
O A:HOH2011 2.1 16.9 1.0
O A:ASP43 2.1 15.3 1.0
OD1 A:ASP176 2.1 15.3 1.0
O A:HOH2008 2.1 14.9 1.0
CG A:ASP41 3.1 17.1 1.0
CG A:ASP176 3.2 14.5 1.0
C A:ASP43 3.3 13.1 1.0
OD1 A:ASP41 3.5 17.0 1.0
OD2 A:ASP176 3.5 16.6 1.0
OD1 A:ASP175 4.0 16.0 1.0
CA A:ASP43 4.1 14.0 1.0
CB A:ASP43 4.2 14.2 1.0
N A:GLY44 4.3 14.0 1.0
N A:ASP43 4.3 13.4 1.0
O2 A:DRM1001 4.3 20.9 1.0
OP1 A:DRM1001 4.3 24.7 1.0
N A:ASP176 4.4 12.5 1.0
CB A:ASP41 4.4 14.8 1.0
CA A:GLY44 4.4 14.7 1.0
CB A:ASP176 4.4 13.0 1.0
OP2 A:DRM1001 4.5 21.6 1.0
CE1 A:PHE75 4.6 20.2 1.0
O A:HOH2232 4.6 34.7 1.0
CZ A:PHE75 4.7 19.6 1.0
CG A:ASP175 4.7 14.9 1.0
CG2 A:VAL45 4.8 13.7 1.0
CA A:ASP176 4.8 13.1 1.0
P A:DRM1001 4.9 19.8 1.0
N A:ARG177 4.9 12.7 1.0
C A:GLY44 4.9 15.7 1.0
C A:MET42 5.0 13.2 1.0
OD2 A:ASP175 5.0 17.6 1.0

Reference:

A.Rinaldo-Matthis, C.Rampazzo, J.Balzarini, P.Reichard, V.Bianchi, P.Nordlund. Crystal Structures of the Mitochondrial Deoxyribonucleotidase in Complex with Two Specific Inhibitors Mol.Pharmacol. V. 65 860 2004.
ISSN: ISSN 0026-895X
PubMed: 15044615
DOI: 10.1124/MOL.65.4.860
Page generated: Mon Dec 14 06:38:18 2020

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