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Magnesium in PDB 5tye: Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min)

Enzymatic activity of Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min)

All present enzymatic activity of Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min):
2.7.7.7;

Protein crystallography data

The structure of Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min), PDB code: 5tye was solved by J.A.Jamsen, S.H.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.36 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.998, 68.573, 110.478, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 22.8

Other elements in 5tye:

The structure of Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min) also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min) (pdb code 5tye). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min), PDB code: 5tye:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5tye

Go back to Magnesium Binding Sites List in 5tye
Magnesium binding site 1 out of 2 in the Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:19.4
occ:1.00
O A:HOH709 2.0 26.5 0.7
O A:HOH666 2.1 19.9 1.0
OD1 A:ASP330 2.1 23.2 1.0
OD2 A:ASP332 2.1 19.4 1.0
OP1 P:DT5 2.1 19.5 1.0
O32 A:PPV512 2.1 18.2 0.8
O31 A:PPV512 2.8 27.3 0.3
CG A:ASP330 3.0 30.8 1.0
CG A:ASP332 3.2 20.6 1.0
P2 A:PPV512 3.2 25.4 0.8
OD2 A:ASP330 3.4 33.0 1.0
OPP A:PPV512 3.4 29.7 0.8
MG A:MG502 3.4 16.7 0.7
NA A:NA503 3.4 19.1 0.3
P P:DT5 3.5 21.6 1.0
OD1 A:ASP332 3.6 16.6 1.0
P1 A:PPV512 3.7 29.9 0.3
O22 A:PPV512 3.9 33.1 0.8
O5' P:DT5 4.0 18.7 1.0
O A:ASP330 4.1 19.8 1.0
C5' P:DT5 4.1 17.7 1.0
O A:HOH602 4.2 34.8 1.0
O A:HOH610 4.2 19.5 1.0
N A:GLY320 4.3 14.9 1.0
O A:HOH801 4.4 30.3 1.0
CB A:ASP330 4.4 22.8 1.0
O A:HOH627 4.4 28.1 1.0
OP2 P:DT5 4.4 20.8 1.0
C A:ASP330 4.5 21.1 1.0
CB A:ASP332 4.5 17.8 1.0
O12 A:PPV512 4.5 18.7 0.8
O3' P:DA4 4.5 20.5 1.0
CA A:GLY319 4.5 16.9 1.0
O21 A:PPV512 4.7 28.5 0.3
O11 A:PPV512 4.7 27.6 0.3
CA A:ASP330 4.9 23.4 1.0

Magnesium binding site 2 out of 2 in 5tye

Go back to Magnesium Binding Sites List in 5tye
Magnesium binding site 2 out of 2 in the Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Dna Polymerase Mu Product Complex, 10 Mm MG2+ (60 Min) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:16.7
occ:0.74
NA A:NA503 0.0 19.1 0.3
OD1 A:ASP332 2.1 16.6 1.0
OD2 A:ASP418 2.2 19.9 1.0
OP1 P:DT5 2.3 19.5 1.0
OD1 A:ASP330 2.6 23.2 1.0
O A:HOH627 2.7 28.1 1.0
O3' P:DA4 2.7 20.5 1.0
CG A:ASP332 3.1 20.6 1.0
P P:DT5 3.1 21.6 1.0
CG A:ASP330 3.2 30.8 1.0
CG A:ASP418 3.2 20.5 1.0
OD2 A:ASP332 3.3 19.4 1.0
MG A:MG501 3.4 19.4 1.0
OD2 A:ASP330 3.7 33.0 1.0
CB A:ASP418 3.8 19.4 1.0
C3' P:DA4 3.9 18.7 1.0
CB A:ASP330 4.0 22.8 1.0
C4' P:DA4 4.0 19.2 1.0
C5' P:DA4 4.0 21.1 1.0
OP2 P:DT5 4.1 20.8 1.0
OD1 A:ASP418 4.2 21.1 1.0
O5' P:DT5 4.3 18.7 1.0
CB A:ASP332 4.4 17.8 1.0
C5' P:DT5 4.4 17.7 1.0
NH2 A:ARG416 4.5 18.2 1.0
O A:HOH709 4.6 26.5 0.7
O A:VAL331 4.6 18.1 1.0
CZ3 A:TRP434 4.8 19.0 1.0
O5' P:DA4 4.9 21.8 1.0
C A:VAL331 4.9 20.1 1.0
N A:ASP418 4.9 16.9 1.0
CA A:ASP332 4.9 18.2 1.0
OP1 P:DA4 5.0 20.1 1.0
O A:HOH666 5.0 19.9 1.0

Reference:

J.A.Jamsen, W.A.Beard, L.C.Pedersen, D.D.Shock, A.F.Moon, J.M.Krahn, K.Bebenek, T.A.Kunkel, S.H.Wilson. Time-Lapse Crystallography Snapshots of A Double-Strand Break Repair Polymerase in Action. Nat Commun V. 8 253 2017.
ISSN: ESSN 2041-1723
PubMed: 28811466
DOI: 10.1038/S41467-017-00271-7
Page generated: Mon Sep 30 05:05:51 2024

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