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Magnesium in PDB 4g7z: Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1

Enzymatic activity of Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1

All present enzymatic activity of Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1, PDB code: 4g7z was solved by Y.Zhang, R.H.Ebright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.85 / 3.81
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 185.465, 103.590, 296.507, 90.00, 98.53, 90.00
R / Rfree (%) 17.6 / 23.2

Other elements in 4g7z:

The structure of Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1 also contains other interesting chemical elements:

Bromine (Br) 2 atoms
Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1 (pdb code 4g7z). 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 Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1, PDB code: 4g7z:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4g7z

Go back to Magnesium Binding Sites List in 4g7z
Magnesium binding site 1 out of 2 in the Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1


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 Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2003

b:0.6
occ:1.00
OD1 D:ASP743 2.2 0.1 1.0
OD2 D:ASP741 2.2 0.5 1.0
OD1 D:ASP741 2.3 0.7 1.0
OD1 D:ASP739 2.4 0.1 1.0
OD2 D:ASP739 2.4 0.6 1.0
OD2 D:ASP743 2.5 0.5 1.0
CG D:ASP741 2.5 0.9 1.0
CG D:ASP743 2.6 0.9 1.0
CG D:ASP739 2.7 0.2 1.0
CB D:ASP743 4.0 0.6 1.0
CB D:ASP741 4.0 0.7 1.0
CB D:ASP739 4.1 0.4 1.0
NH2 D:ARG704 4.3 0.9 1.0
N D:ASP739 4.3 0.6 1.0
O D:ASP739 4.4 0.2 1.0
N D:ASP741 4.5 0.6 1.0
C D:ASP739 4.6 0.7 1.0
CA D:ASP739 4.6 0.7 1.0
CA D:ASP743 4.8 0.3 1.0
CA D:ASP741 4.8 0.0 1.0
N D:ASP743 4.9 1.0 1.0
NE D:ARG704 5.0 0.3 1.0

Magnesium binding site 2 out of 2 in 4g7z

Go back to Magnesium Binding Sites List in 4g7z
Magnesium binding site 2 out of 2 in the Crystal Structure of Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1


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 Thermus Thermophilus Transcription Initiation Complex Containing 5-Bru at Template-Strand Position +1 within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Mg2003

b:0.1
occ:1.00
OD1 N:ASP739 2.0 0.8 1.0
OD1 N:ASP743 2.2 0.1 1.0
OD2 N:ASP741 2.2 0.3 1.0
OD1 N:ASP741 2.2 0.4 1.0
OD2 N:ASP743 2.3 0.8 1.0
OD2 N:ASP739 2.3 0.2 1.0
CG N:ASP739 2.4 0.6 1.0
CG N:ASP743 2.5 0.4 1.0
CG N:ASP741 2.5 0.7 1.0
CB N:ASP739 3.9 0.7 1.0
CB N:ASP743 4.0 0.3 1.0
CB N:ASP741 4.0 0.3 1.0
N N:ASP739 4.2 0.8 1.0
O N:ASP739 4.2 0.8 1.0
N N:ASP741 4.4 0.3 1.0
C N:ASP739 4.5 0.1 1.0
CA N:ASP739 4.5 0.6 1.0
NH2 N:ARG704 4.5 0.8 1.0
CA N:ASP741 4.7 0.6 1.0
N N:ASP743 4.8 0.7 1.0
CA N:ASP743 4.8 0.0 1.0

Reference:

Y.Zhang, Y.Feng, S.Chatterjee, S.Tuske, M.X.Ho, E.Arnold, R.H.Ebright. Structural Basis of Transcription Initiation. Science V. 338 1076 2012.
ISSN: ISSN 0036-8075
PubMed: 23086998
DOI: 10.1126/SCIENCE.1227786
Page generated: Mon Aug 11 13:11:58 2025

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