Magnesium in PDB 5tws: Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp

Protein crystallography data

The structure of Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp, PDB code: 5tws was solved by A.F.Moon, J.M.Pryor, D.A.Ramsden, T.A.Kunkel, K.Bebenek, L.C.Pedersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.48 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.935, 68.858, 110.319, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 20

Other elements in 5tws:

The structure of Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms
Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp (pdb code 5tws). 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 Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp, PDB code: 5tws:

Magnesium binding site 1 out of 1 in 5tws

Go back to Magnesium Binding Sites List in 5tws
Magnesium binding site 1 out of 1 in the Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Post-Catalytic Complex of Human Polymerase Mu (H329A) with Newly Incorporated Utp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:12.8
occ:1.00
OD2 A:ASP332 2.1 12.6 1.0
OP1 P:U5 2.1 12.8 1.0
O12 A:GOA503 2.1 13.8 0.9
O A:HOH735 2.1 14.5 1.0
OD1 A:ASP330 2.1 14.5 1.0
O2 A:GOA503 2.2 17.8 0.9
C1 A:GOA503 2.9 12.6 0.9
C2 A:GOA503 3.0 23.3 0.9
CG A:ASP332 3.1 13.7 1.0
CG A:ASP330 3.1 22.2 1.0
NA A:NA502 3.3 12.0 1.0
P P:U5 3.4 12.6 1.0
OD2 A:ASP330 3.5 24.2 1.0
OD1 A:ASP332 3.5 14.0 1.0
O5' P:U5 3.9 10.9 1.0
O A:HOH805 4.0 22.5 1.0
C5' P:U5 4.0 10.1 1.0
O11 A:GOA503 4.1 12.4 0.9
O A:ASP330 4.2 12.4 1.0
O A:HOH634 4.3 11.3 1.0
N A:GLY320 4.3 7.8 1.0
OP2 P:U5 4.3 12.2 1.0
O P:HOH102 4.4 32.5 1.0
CB A:ASP332 4.4 9.0 1.0
O P:HOH107 4.4 27.0 1.0
CB A:ASP330 4.5 13.9 1.0
O3' P:DA4 4.5 11.1 1.0
C A:ASP330 4.5 12.8 1.0
CA A:GLY319 4.6 8.7 1.0
O A:HOH732 4.6 26.7 1.0
N A:ASP332 4.9 10.1 1.0
CA A:ASP330 5.0 12.7 1.0

Reference:

A.F.Moon, J.M.Pryor, D.A.Ramsden, T.A.Kunkel, K.Bebenek, L.C.Pedersen. Structural Accommodation of Ribonucleotide Incorporation By the Dna Repair Enzyme Polymerase Mu. Nucleic Acids Res. V. 45 9138 2017.
ISSN: ESSN 1362-4962
PubMed: 28911097
DOI: 10.1093/NAR/GKX527
Page generated: Mon Dec 14 21:13:12 2020

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