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Magnesium in PDB 4ep4: Thermus Thermophilus Ruvc Structure

Enzymatic activity of Thermus Thermophilus Ruvc Structure

All present enzymatic activity of Thermus Thermophilus Ruvc Structure:
3.1.22.4;

Protein crystallography data

The structure of Thermus Thermophilus Ruvc Structure, PDB code: 4ep4 was solved by L.Chen, K.Shi, Z.Q.Yin, H.Aihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.48 / 1.28
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.777, 51.151, 134.910, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 19.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Thermus Thermophilus Ruvc Structure (pdb code 4ep4). 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 Thermus Thermophilus Ruvc Structure, PDB code: 4ep4:

Magnesium binding site 1 out of 1 in 4ep4

Go back to Magnesium Binding Sites List in 4ep4
Magnesium binding site 1 out of 1 in the Thermus Thermophilus Ruvc Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Thermus Thermophilus Ruvc Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg201

b:21.4
occ:1.00
ND1 B:HIS143 2.0 22.9 1.0
OD2 B:ASP7 2.1 20.4 1.0
O B:HOH328 2.2 31.7 1.0
O B:HOH448 2.4 27.9 1.0
CE1 B:HIS143 2.8 22.1 1.0
CG B:ASP7 3.1 17.3 1.0
CG B:HIS143 3.1 20.5 1.0
OD1 B:ASP7 3.6 20.4 1.0
CB B:HIS143 3.6 16.6 1.0
CA B:HIS143 4.0 14.2 1.0
NE2 B:HIS143 4.0 25.8 1.0
O B:HOH449 4.1 37.1 1.0
CD2 B:HIS143 4.2 25.2 1.0
O B:HOH468 4.2 36.6 1.0
CB B:ASP7 4.3 12.0 1.0
O B:ASP7 4.6 8.7 1.0
OD2 B:ASP146 4.7 29.5 1.0
O B:HIS12 4.8 12.4 1.0
N B:HIS143 4.8 15.4 1.0
CB B:HIS12 4.9 11.3 1.0
O B:PRO8 5.0 16.0 1.0

Reference:

L.Chen, K.Shi, Z.Yin, H.Aihara. Structural Asymmetry in the Thermus Thermophilus Ruvc Dimer Suggests A Basis For Sequential Strand Cleavages During Holliday Junction Resolution. Nucleic Acids Res. V. 41 648 2013.
ISSN: ISSN 0305-1048
PubMed: 23118486
DOI: 10.1093/NAR/GKS1015
Page generated: Mon Aug 11 12:29:30 2025

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