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Magnesium in PDB 2a6h: Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Sterptolydigin

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

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

Protein crystallography data

The structure of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Sterptolydigin, PDB code: 2a6h was solved by D.Temiakov, N.Zenkin, M.N.Vassylyeva, A.Perederina, T.H.Tahirov, M.Savkina, S.Zorov, V.Nikiforov, N.Igarashi, N.Matsugaki, S.Wakatsuki, K.Severinov, D.G.Vassylyev, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.40
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 239.500, 239.500, 253.100, 90.00, 90.00, 120.00
R / Rfree (%) 23 / 26.8

Other elements in 2a6h:

The structure of Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Sterptolydigin 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 Sterptolydigin (pdb code 2a6h). 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 Sterptolydigin, PDB code: 2a6h:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2a6h

Go back to Magnesium Binding Sites List in 2a6h
Magnesium binding site 1 out of 2 in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Sterptolydigin


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 Sterptolydigin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg9001

b:29.2
occ:1.00
OD1 D:ASP741 2.2 54.4 1.0
OD1 D:ASP743 2.3 52.8 1.0
OD1 D:ASP739 2.4 56.6 1.0
CG D:ASP741 3.0 53.2 1.0
OD2 D:ASP741 3.1 53.5 1.0
CG D:ASP739 3.3 53.6 1.0
CG D:ASP743 3.5 50.5 1.0
OD2 D:ASP739 3.5 54.2 1.0
OD2 D:ASP743 4.0 51.0 1.0
CB D:ASP741 4.4 49.0 1.0
N D:ASP741 4.6 42.4 1.0
O D:ASP739 4.6 46.6 1.0
CB D:ASP743 4.6 48.4 1.0
CB D:ASP739 4.7 53.0 1.0
N D:ASP743 4.8 43.8 1.0
CA D:ASP741 4.8 44.4 1.0
C D:ASP741 4.8 44.0 1.0
O D:HOH2214 5.0 53.8 1.0
C D:ASP739 5.0 47.4 1.0

Magnesium binding site 2 out of 2 in 2a6h

Go back to Magnesium Binding Sites List in 2a6h
Magnesium binding site 2 out of 2 in the Crystal Structure of the T. Thermophilus Rna Polymerase Holoenzyme in Complex with Antibiotic Sterptolydigin


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 Sterptolydigin within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Mg9002

b:53.4
occ:1.00
OD1 N:ASP739 2.2 50.9 1.0
OD1 N:ASP743 2.3 52.4 1.0
OD1 N:ASP741 2.3 60.6 1.0
CG N:ASP743 3.1 54.4 1.0
CG N:ASP741 3.2 59.1 1.0
OD2 N:ASP743 3.2 54.7 1.0
CG N:ASP739 3.3 47.9 1.0
OD2 N:ASP741 3.3 59.6 1.0
OD2 N:ASP739 4.1 46.1 1.0
CB N:ASP739 4.1 49.4 1.0
O N:ASP739 4.2 48.9 1.0
C N:ASP739 4.5 50.4 1.0
CB N:ASP743 4.6 55.1 1.0
N N:ASP739 4.6 49.5 1.0
CB N:ASP741 4.6 56.6 1.0
N N:ASP741 4.6 52.2 1.0
CA N:ASP739 4.6 49.4 1.0

Reference:

D.Temiakov, N.Zenkin, M.N.Vassylyeva, A.Perederina, T.H.Tahirov, E.Kashkina, M.Savkina, S.Zorov, V.Nikiforov, N.Igarashi, N.Matsugaki, S.Wakatsuki, K.Severinov, D.G.Vassylyev. Structural Basis of Transcription Inhibition By Antibiotic Streptolydigin. Mol.Cell V. 19 655 2005.
ISSN: ISSN 1097-2765
PubMed: 16167380
DOI: 10.1016/J.MOLCEL.2005.07.020
Page generated: Tue Aug 13 21:27:06 2024

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