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Magnesium in PDB 3maq: Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex

Enzymatic activity of Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex

All present enzymatic activity of Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex, PDB code: 3maq was solved by W.Yang, F.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 80.931, 100.727, 126.223, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 22.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex (pdb code 3maq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex, PDB code: 3maq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3maq

Go back to Magnesium Binding Sites List in 3maq
Magnesium binding site 1 out of 2 in the Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:30.3
occ:1.00
OD1 A:ASP547 1.9 31.0 1.0
O A:TYR420 2.1 11.7 1.0
O1G A:DGT914 2.2 20.9 1.0
OD2 A:ASP419 2.3 21.8 1.0
O2B A:DGT914 2.3 17.0 1.0
O2A A:DGT914 2.3 18.2 1.0
CG A:ASP547 3.1 26.9 1.0
PB A:DGT914 3.2 21.3 1.0
O3A A:DGT914 3.3 23.4 1.0
PG A:DGT914 3.3 19.3 1.0
C A:TYR420 3.3 13.1 1.0
CG A:ASP419 3.4 20.9 1.0
PA A:DGT914 3.4 22.2 1.0
O3B A:DGT914 3.5 23.0 1.0
O A:HOH1043 3.8 34.2 1.0
OD2 A:ASP547 3.8 26.2 1.0
OD1 A:ASP419 3.9 23.3 1.0
MG A:MG1002 3.9 34.9 1.0
O A:HOH998 3.9 32.1 1.0
O2G A:DGT914 4.0 18.9 1.0
N A:TYR420 4.0 12.9 1.0
N A:SER422 4.0 13.3 1.0
CA A:TYR420 4.1 12.2 1.0
O5' A:DGT914 4.1 23.4 1.0
CB A:ASP547 4.2 24.8 1.0
N A:LYS421 4.3 13.0 1.0
O1A A:DGT914 4.3 19.9 1.0
C A:ASP419 4.4 13.4 1.0
C5' A:DGT914 4.4 24.4 1.0
CA A:LYS421 4.4 13.2 1.0
O3G A:DGT914 4.5 21.4 1.0
C A:LYS421 4.5 12.6 1.0
O1B A:DGT914 4.6 21.5 1.0
N A:LEU423 4.6 12.1 1.0
CB A:ASP419 4.6 16.0 1.0
CB A:TYR420 4.6 13.8 1.0
O A:ASP419 4.8 12.1 1.0
CA A:SER422 4.8 12.8 1.0
CA A:ASP419 5.0 13.7 1.0

Magnesium binding site 2 out of 2 in 3maq

Go back to Magnesium Binding Sites List in 3maq
Magnesium binding site 2 out of 2 in the Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of E.Coli Pol II-Normal Dna-Dgtp Ternary Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:34.9
occ:1.00
OD2 A:ASP547 2.2 26.2 1.0
O2A A:DGT914 2.3 18.2 1.0
O A:HOH1003 2.4 32.1 1.0
OD1 A:ASP419 2.4 23.3 1.0
O A:HOH1139 2.6 26.9 1.0
CG A:ASP547 3.1 26.9 1.0
OD1 A:ASP547 3.2 31.0 1.0
CG A:ASP419 3.4 20.9 1.0
C3' P:DOC913 3.4 18.9 1.0
PA A:DGT914 3.4 22.2 1.0
OD2 A:ASP419 3.6 21.8 1.0
O1A A:DGT914 3.7 19.9 1.0
O5' A:DGT914 3.7 23.4 1.0
O A:HOH1043 3.8 34.2 1.0
MG A:MG1001 3.9 30.3 1.0
O P:HOH232 4.1 33.7 1.0
C5' P:DOC913 4.2 18.6 1.0
C4' P:DOC913 4.2 17.7 1.0
O A:ASP545 4.3 19.7 1.0
CB A:SER548 4.3 21.4 1.0
C5' A:DGT914 4.4 24.4 1.0
CB A:ASP547 4.5 24.8 1.0
C A:ASP547 4.6 22.8 1.0
N A:SER548 4.7 22.3 1.0
CB A:ASP419 4.7 16.0 1.0
N A:ASP547 4.7 20.1 1.0
C2' P:DOC913 4.7 19.4 1.0
O3A A:DGT914 4.8 23.4 1.0
O5' P:DOC913 4.8 20.7 1.0
CA A:ASP547 4.9 22.2 1.0
O1G A:DGT914 4.9 20.9 1.0
O A:ASP547 4.9 22.5 1.0

Reference:

F.Wang, W.Yang. Structural Insight Into Translesion Synthesis By Dna Pol II Cell(Cambridge,Mass.) V. 139 1279 2009.
ISSN: ISSN 0092-8674
PubMed: 20064374
DOI: 10.1016/J.CELL.2009.11.043
Page generated: Mon Aug 11 00:30:43 2025

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