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Magnesium in PDB 6vw0: Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex

Enzymatic activity of Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex

All present enzymatic activity of Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex:
2.7.7.6;

Other elements in 6vw0:

The structure of Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex (pdb code 6vw0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex, PDB code: 6vw0:

Magnesium binding site 1 out of 1 in 6vw0

Go back to Magnesium Binding Sites List in 6vw0
Magnesium binding site 1 out of 1 in the Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Tuberculosis Rnap S456L Mutant Open Promoter Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2002

b:98.8
occ:1.00
OD1 D:ASP537 2.1 91.4 1.0
OD1 D:ASP535 2.1 92.3 1.0
OD2 D:ASP537 2.1 91.4 1.0
OD2 D:ASP535 2.2 92.3 1.0
CG D:ASP535 2.4 92.3 1.0
CG D:ASP537 2.4 91.4 1.0
OD1 D:ASP539 3.2 89.4 1.0
OD2 D:ASP539 3.8 89.4 1.0
CB D:ASP535 3.8 92.3 1.0
CG D:ASP539 3.9 89.4 1.0
CB D:ASP537 3.9 91.4 1.0
N D:ASP537 4.5 91.4 1.0
CA D:ASP535 4.6 92.3 1.0
N D:ASP535 4.6 92.3 1.0
C D:ASP535 4.6 92.3 1.0
NH2 D:ARG500 4.7 83.5 1.0
CA D:ASP537 4.7 91.4 1.0
O D:ASP535 4.7 92.3 1.0

Reference:

M.Lilic, J.Chen, H.Boyaci, N.Braffman, E.A.Hubin, J.Herrmann, R.Muller, R.Mooney, R.Landick, S.A.Darst, E.A.Campbell. The Antibiotic Sorangicin A Inhibits Promoter Dna Unwinding in A Mycobacterium Tuberculosis Rifampicin-Resistant Rna Polymerase. Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
PubMed: 33199626
DOI: 10.1073/PNAS.2013706117
Page generated: Tue Oct 1 22:16:05 2024

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