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Magnesium in PDB 8t3x: Tna Polymerase, Closed Ternary

Protein crystallography data

The structure of Tna Polymerase, Closed Ternary, PDB code: 8t3x was solved by V.Maola, J.Chaput, N.Chim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.39 / 2.73
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.869, 99.525, 110.727, 90, 90, 90
R / Rfree (%) 24.2 / 30.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Tna Polymerase, Closed Ternary (pdb code 8t3x). 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 Tna Polymerase, Closed Ternary, PDB code: 8t3x:

Magnesium binding site 1 out of 1 in 8t3x

Go back to Magnesium Binding Sites List in 8t3x
Magnesium binding site 1 out of 1 in the Tna Polymerase, Closed Ternary


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tna Polymerase, Closed Ternary within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:38.4
occ:1.00
OD2 A:ASP543 2.0 40.1 1.0
OD2 A:ASP405 2.1 42.5 1.0
O3A A:9O7801 2.2 41.3 1.0
O2G A:9O7801 2.4 40.8 1.0
O A:PHE406 2.4 39.0 1.0
O2B A:9O7801 3.0 40.9 1.0
PB A:9O7801 3.1 40.3 1.0
CG A:ASP543 3.2 39.9 1.0
CG A:ASP405 3.2 43.1 1.0
PA A:9O7801 3.3 41.6 1.0
O3B A:9O7801 3.5 39.6 1.0
PG A:9O7801 3.5 39.7 1.0
C A:PHE406 3.6 38.5 1.0
O1A A:9O7801 3.6 42.4 1.0
OD1 A:ASP405 3.7 42.5 1.0
OD1 A:ASP543 3.8 39.4 1.0
N A:PHE406 4.1 38.8 1.0
C3' A:9O7801 4.1 42.6 1.0
O3' A:9O7801 4.2 42.4 1.0
CA A:PHE406 4.3 38.8 1.0
CB A:ASP543 4.3 38.8 1.0
N A:SER408 4.4 38.5 1.0
O1B A:9O7801 4.4 39.9 1.0
CB A:ASP405 4.4 44.9 1.0
O1G A:9O7801 4.4 39.4 1.0
N A:ARG407 4.6 39.7 1.0
O3G A:9O7801 4.6 39.6 1.0
CB A:PHE406 4.7 37.8 1.0
O2A A:9O7801 4.7 41.0 1.0
N A:LEU409 4.7 38.1 1.0
C A:ASP405 4.8 42.0 1.0
CA A:ARG407 4.8 39.6 1.0
O A:ASP543 4.8 39.4 1.0
C A:ARG407 5.0 38.6 1.0

Reference:

V.Maola, E.Yik, M.Hajjar, J.Lee, M.Holguin, R.Quijano, K.Nguyen, K.Ho, J.Medina, N.Chim, J.Chaput. Directed Evolution of A Highly Efficient Tna Polymerase Achieved By Homologous Recombination To Be Published.
Page generated: Fri Oct 4 20:18:32 2024

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