Magnesium in PDB 3eql: Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin

Enzymatic activity of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin

All present enzymatic activity of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin, PDB code: 3eql was solved by D.G.Vassylyev, M.N.Vassylyeva, I.Artsimovitch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.70
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 235.001, 235.001, 254.947, 90.00, 90.00, 120.00
R / Rfree (%) 24 / 27

Other elements in 3eql:

The structure of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin (pdb code 3eql). 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 the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin, PDB code: 3eql:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3eql

Go back to Magnesium Binding Sites List in 3eql
Magnesium binding site 1 out of 2 in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin


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 the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1528

b:35.2
occ:1.00
OD2 D:ASP741 2.1 42.8 1.0
OD1 D:ASP743 2.1 31.5 1.0
OD2 D:ASP739 2.2 43.3 1.0
CG D:ASP741 2.6 37.5 1.0
OD1 D:ASP741 2.9 36.7 1.0
CG D:ASP743 3.1 33.6 1.0
CG D:ASP739 3.4 41.4 1.0
OD2 D:ASP743 3.4 35.6 1.0
CB D:ASP741 3.7 32.0 1.0
CB D:ASP739 4.2 34.6 1.0
OD1 D:ASP739 4.3 47.6 1.0
N D:ASP741 4.4 27.1 1.0
O D:ASP739 4.4 30.3 1.0
CA D:ASP741 4.5 28.4 1.0
CB D:ASP743 4.5 31.4 1.0
N D:ASP743 4.6 28.2 1.0
C D:ASP741 4.6 28.0 1.0
C D:ASP739 4.7 30.0 1.0
N D:ASP739 4.7 29.4 1.0
CA D:ASP739 4.8 30.5 1.0
O D:HOH1599 4.8 18.5 1.0
N D:GLY742 4.9 27.7 1.0

Magnesium binding site 2 out of 2 in 3eql

Go back to Magnesium Binding Sites List in 3eql
Magnesium binding site 2 out of 2 in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin


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 the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Myxopyronin within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Mg1528

b:41.4
occ:1.00
OD2 N:ASP739 2.2 47.6 1.0
OD1 N:ASP743 2.2 31.7 1.0
OD2 N:ASP741 2.2 38.5 1.0
OD1 N:ASP741 2.3 32.7 1.0
CG N:ASP741 2.3 34.4 1.0
CG N:ASP743 3.3 29.4 1.0
CG N:ASP739 3.4 44.3 1.0
OD2 N:ASP743 3.6 28.6 1.0
CB N:ASP741 3.6 29.4 1.0
O N:HOH1932 3.6 34.9 1.0
CB N:ASP739 4.3 38.3 1.0
OD1 N:ASP739 4.3 48.1 1.0
N N:ASP741 4.4 24.9 1.0
CA N:ASP741 4.4 25.8 1.0
O N:ASP739 4.6 34.0 1.0
CB N:ASP743 4.6 28.1 1.0
C N:ASP741 4.6 24.7 1.0
N N:ASP743 4.7 27.3 1.0
C N:ASP739 4.8 32.7 1.0
N N:ASP739 4.8 34.5 1.0
CA N:ASP739 4.9 34.3 1.0
O M:HOH2110 5.0 45.9 1.0
N N:GLY742 5.0 24.1 1.0
O N:ASP741 5.0 23.9 1.0

Reference:

G.A.Belogurov, M.N.Vassylyeva, A.Sevostyanova, J.R.Appleman, A.X.Xiang, R.Lira, S.E.Webber, S.Klyuyev, E.Nudler, I.Artsimovitch, D.G.Vassylyev. Transcription Inactivation Through Local Refolding of the Rna Polymerase Structure. Nature V. 457 332 2009.
ISSN: ISSN 0028-0836
PubMed: 18946472
DOI: 10.1038/NATURE07510
Page generated: Mon Dec 14 08:07:00 2020

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