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Magnesium in PDB 5uhf: Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336, PDB code: 5uhf was solved by W.Lin, K.Das, Y.Feng, R.H.Ebright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.50 / 4.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 152.374, 163.460, 197.384, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 26.7

Other elements in 5uhf:

The structure of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336 (pdb code 5uhf). 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 Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336, PDB code: 5uhf:

Magnesium binding site 1 out of 1 in 5uhf

Go back to Magnesium Binding Sites List in 5uhf
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336


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 Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-IX336 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1403

b:28.2
occ:1.00
OD1 D:ASP537 2.0 32.3 1.0
OD1 D:ASP535 2.2 29.9 1.0
OD1 D:ASP539 2.5 28.4 1.0
OD2 D:ASP537 2.6 31.3 1.0
CG D:ASP537 2.6 32.4 1.0
CG D:ASP535 3.1 31.5 1.0
OD2 D:ASP535 3.3 31.2 1.0
CG D:ASP539 3.4 27.8 1.0
OD2 D:ASP539 3.6 28.9 1.0
CB D:ASP537 4.1 35.4 1.0
CB D:ASP535 4.4 32.8 1.0
NH2 D:ARG500 4.4 32.7 1.0
N D:ASP537 4.6 33.5 1.0
O D:ASP537 4.7 34.8 1.0
O D:ASP535 4.7 32.7 1.0
CA D:ASP537 4.7 35.7 1.0
CB D:ASP539 4.8 27.5 1.0
C D:ASP537 4.8 34.2 1.0
C D:ASP535 4.9 34.2 1.0
N D:ASP535 5.0 35.4 1.0

Reference:

W.Lin, S.Mandal, D.Degen, Y.Liu, Y.W.Ebright, S.Li, Y.Feng, Y.Zhang, S.Mandal, Y.Jiang, S.Liu, M.Gigliotti, M.Talaue, N.Connell, K.Das, E.Arnold, R.H.Ebright. Structural Basis of Mycobacterium Tuberculosis Transcription and Transcription Inhibition. Mol. Cell V. 66 169 2017.
ISSN: ISSN 1097-4164
PubMed: 28392175
DOI: 10.1016/J.MOLCEL.2017.03.001
Page generated: Mon Sep 30 05:20:16 2024

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