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Magnesium in PDB 1q5h: Human Dutp Pyrophosphatase Complex with Dudp

Protein crystallography data

The structure of Human Dutp Pyrophosphatase Complex with Dudp, PDB code: 1q5h was solved by C.D.Mol, J.M.Harris, E.M.Mcintosh, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.197, 110.766, 53.243, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Dutp Pyrophosphatase Complex with Dudp (pdb code 1q5h). 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 Human Dutp Pyrophosphatase Complex with Dudp, PDB code: 1q5h:

Magnesium binding site 1 out of 1 in 1q5h

Go back to Magnesium Binding Sites List in 1q5h
Magnesium binding site 1 out of 1 in the Human Dutp Pyrophosphatase Complex with Dudp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Dutp Pyrophosphatase Complex with Dudp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg999

b:15.3
occ:1.00
OE1 B:GLU112 2.2 5.2 1.0
O A:HOH1012 2.3 16.8 1.0
OE1 C:GLU112 2.3 7.9 1.0
OE1 A:GLU112 2.3 11.1 1.0
CD B:GLU112 3.2 6.2 1.0
CD C:GLU112 3.2 7.1 1.0
CD A:GLU112 3.3 10.6 1.0
CB B:GLU112 3.6 5.7 1.0
CB C:GLU112 3.6 6.4 1.0
O C:HOH787 3.6 15.9 1.0
CB A:GLU112 3.6 7.4 1.0
CG B:GLU112 3.9 5.4 1.0
CG C:GLU112 3.9 6.2 1.0
CG A:GLU112 4.0 8.5 1.0
OE2 C:GLU112 4.0 8.2 1.0
OE2 B:GLU112 4.1 5.5 1.0
OE2 A:GLU112 4.1 9.7 1.0
CA B:GLU112 4.4 5.2 1.0
CA A:GLU112 4.5 6.9 1.0
CA C:GLU112 4.5 6.0 1.0
O B:ARG113 4.6 5.2 1.0
O C:ARG113 4.6 6.0 1.0
O A:ARG113 4.6 7.3 1.0
C B:GLU112 4.8 5.1 1.0
N B:ARG113 4.8 4.8 1.0
C A:GLU112 4.9 6.8 1.0
N A:ARG113 4.9 6.5 1.0

Reference:

C.D.Mol, J.M.Harris, E.M.Mcintosh, J.A.Tainer. Human Dutp Pyrophosphatase: Uracil Recognition By A Beta Hairpin and Active Sites Formed By Three Separate Subunits Structure V. 4 1077 1996.
ISSN: ISSN 0969-2126
PubMed: 8805593
DOI: 10.1016/S0969-2126(96)00114-1
Page generated: Mon Dec 14 06:37:02 2020

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