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Magnesium in PDB 2rgr: Topoisomerase Iia Bound to G-Segment Dna

Enzymatic activity of Topoisomerase Iia Bound to G-Segment Dna

All present enzymatic activity of Topoisomerase Iia Bound to G-Segment Dna:
5.99.1.3;

Protein crystallography data

The structure of Topoisomerase Iia Bound to G-Segment Dna, PDB code: 2rgr was solved by K.C.Dong, J.M.Berger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.87 / 3.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 85.435, 126.801, 223.492, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 27.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Topoisomerase Iia Bound to G-Segment Dna (pdb code 2rgr). 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 Topoisomerase Iia Bound to G-Segment Dna, PDB code: 2rgr:

Magnesium binding site 1 out of 1 in 2rgr

Go back to Magnesium Binding Sites List in 2rgr
Magnesium binding site 1 out of 1 in the Topoisomerase Iia Bound to G-Segment Dna


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Topoisomerase Iia Bound to G-Segment Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:30.1
occ:1.00
O A:HOH30 1.9 80.7 1.0
O A:HOH31 2.1 67.4 1.0
OD2 A:ASP528 2.2 38.9 1.0
O C:HOH45 2.3 56.8 1.0
O A:HOH32 2.4 55.4 1.0
OD1 A:ASP526 3.1 61.4 1.0
CG A:ASP528 3.1 40.3 1.0
OD2 A:ASP526 3.3 59.8 1.0
OD1 A:ASP528 3.4 41.1 1.0
CG A:ASP526 3.5 61.1 1.0
OE2 A:GLU449 3.5 48.1 1.0
OP1 C:DG15 3.8 36.4 1.0
C5' C:DG15 4.3 38.6 1.0
CD A:GLU449 4.4 49.3 1.0
O A:LYS603 4.5 50.1 1.0
O A:HOH2 4.5 22.4 1.0
CB A:ASP528 4.5 41.4 1.0
OE1 A:GLU449 4.6 50.4 1.0
C3' C:DG15 4.8 39.2 1.0
O5' C:DG15 4.9 37.2 1.0
CB A:ASP526 5.0 62.7 1.0
P C:DG15 5.0 36.0 1.0
C4' C:DG15 5.0 39.6 1.0

Reference:

K.C.Dong, J.M.Berger. Structural Basis For Gate-Dna Recognition and Bending By Type Iia Topoisomerases. Nature V. 450 1201 2007.
ISSN: ISSN 0028-0836
PubMed: 18097402
DOI: 10.1038/NATURE06396
Page generated: Mon Dec 14 07:38:36 2020

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