Magnesium in PDB 8e8m: Mycobacterium Tuberculosis Rnap Paused Elongation Complex

Enzymatic activity of Mycobacterium Tuberculosis Rnap Paused Elongation Complex

All present enzymatic activity of Mycobacterium Tuberculosis Rnap Paused Elongation Complex:
2.7.7.6;

Other elements in 8e8m:

The structure of Mycobacterium Tuberculosis Rnap Paused Elongation 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 Paused Elongation Complex (pdb code 8e8m). 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 Paused Elongation Complex, PDB code: 8e8m:

Magnesium binding site 1 out of 1 in 8e8m

Go back to Magnesium Binding Sites List in 8e8m
Magnesium binding site 1 out of 1 in the Mycobacterium Tuberculosis Rnap Paused Elongation 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 Paused Elongation Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2002

b:28.1
occ:1.00
O3' R:U42 2.0 42.0 1.0
OD1 D:ASP535 2.2 41.3 1.0
OD1 D:ASP539 2.3 54.6 1.0
OD2 D:ASP539 2.4 43.3 1.0
OD1 D:ASP537 2.5 47.9 1.0
CG D:ASP535 2.6 43.6 1.0
OD2 D:ASP535 2.6 47.7 1.0
CG D:ASP539 2.7 44.7 1.0
C3' R:U42 3.3 49.8 1.0
CG D:ASP537 3.3 42.1 1.0
OD2 D:ASP537 3.4 37.2 1.0
O2' R:U42 3.5 54.1 1.0
O D:ASP535 3.9 43.0 1.0
C2' R:U42 3.9 51.0 1.0
CB D:ASP535 3.9 33.9 1.0
N D:ASP535 4.0 45.7 1.0
C4' R:U42 4.1 45.1 1.0
C D:ASP535 4.1 35.5 1.0
CB D:ASP539 4.2 32.3 1.0
CA D:ASP535 4.2 36.3 1.0
NH2 D:ARG500 4.5 36.3 1.0
N D:ASP537 4.6 36.9 1.0
CB D:ASP537 4.7 34.8 1.0
C5' R:U42 4.8 43.5 1.0
N D:ASP539 4.8 40.4 1.0
N D:PHE536 4.9 32.7 1.0
CA D:ASP539 4.9 33.0 1.0

Reference:

M.Delbeau, E.A.Campbell, S.A.Darst. Mycobacterium Tuberculosis Rnap Paused Elongation Complex To Be Published.
Page generated: Fri Apr 7 09:23:25 2023

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