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Magnesium in PDB 4qzi: Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+

Enzymatic activity of Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+

All present enzymatic activity of Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+:
2.7.7.31;

Protein crystallography data

The structure of Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+, PDB code: 4qzi was solved by J.Gouge, M.Delarue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.42 / 2.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 57.700, 71.523, 113.035, 90.00, 94.17, 90.00
R / Rfree (%) 18.5 / 20.3

Other elements in 4qzi:

The structure of Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+ also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+ (pdb code 4qzi). 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 Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+, PDB code: 4qzi:

Magnesium binding site 1 out of 1 in 4qzi

Go back to Magnesium Binding Sites List in 4qzi
Magnesium binding site 1 out of 1 in the Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mouse Tdt, F401A Mutant, in Complex with A Dsb Substrate and ZN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:62.3
occ:1.00
 OD1 A:ASP343 2.1 60.8 1.0
O A:HOH722 2.2 44.6 1.0
O2B A:DCT605 2.4 0.3 1.0
OP1 U:DC6 2.5 55.9 1.0
OD2 A:ASP345 2.7 59.8 1.0
O3G A:DCT605 2.9 0.7 1.0
O3B A:DCT605 3.1 0.5 1.0
CG A:ASP343 3.3 60.6 1.0
PB A:DCT605 3.4 0.7 1.0
ZN A:ZN601 3.5 58.4 1.0
PG A:DCT605 3.6 0.5 1.0
CG A:ASP345 3.6 60.8 1.0
P U:DC6 3.9 54.8 1.0
OD1 A:ASP345 3.9 69.0 1.0
OD2 A:ASP343 3.9 63.2 1.0
O A:ASP343 4.0 57.2 1.0
CE1 A:HIS342 4.0 66.8 1.0
ND1 A:HIS342 4.1 67.0 1.0
O A:HOH757 4.1 54.9 1.0
O1G A:DCT605 4.2 0.6 1.0
O3A A:DCT605 4.2 0.3 1.0
O5' U:DC6 4.3 53.9 1.0
C A:ASP343 4.4 56.2 1.0
O A:HOH761 4.4 74.6 1.0
C5' U:DC6 4.5 52.8 1.0
CB A:ASP343 4.5 54.5 1.0
N A:GLY333 4.5 44.7 1.0
N A:ASP343 4.6 54.4 1.0
CA A:GLY332 4.6 47.0 1.0
O1B A:DCT605 4.7 0.8 1.0
OP2 U:DC6 4.7 54.1 1.0
CA A:ASP343 4.7 53.8 1.0
CB A:ASP345 4.8 47.5 1.0
O2G A:DCT605 4.9 0.3 1.0
O3' U:DA5 4.9 56.4 1.0
NE2 A:HIS342 5.0 67.3 1.0

Reference:

J.Gouge, S.Rosario, F.Romain, F.Poitevin, P.Beguin, M.Delarue. Structural Basis For A Novel Mechanism of Dna Bridging and Alignment in Eukaryotic Dsb Dna Repair. Embo J. V. 34 1126 2015.
ISSN: ISSN 0261-4189
PubMed: 25762590
DOI: 10.15252/EMBJ.201489643
Page generated: Mon Aug 11 22:59:44 2025

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