Magnesium in PDB 5uhe: Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-AAP1

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-AAP1

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-AAP1:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-AAP1, PDB code: 5uhe 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) 49.27 / 4.04
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 151.531, 162.155, 195.681, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 25.9

Other elements in 5uhe:

The structure of Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-AAP1 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-AAP1 (pdb code 5uhe). 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-AAP1, PDB code: 5uhe:

Magnesium binding site 1 out of 1 in 5uhe

Go back to Magnesium Binding Sites List in 5uhe
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Transcription Initiation Complex in Complex with D-AAP1


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-AAP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1403

b:19.0
occ:1.00
 OD1 D:ASP537 2.2 25.9 1.0
OD1 D:ASP535 2.4 25.4 1.0
OD1 D:ASP539 2.4 26.6 1.0
CG D:ASP539 3.1 27.9 1.0
OD2 D:ASP539 3.1 29.3 1.0
CG D:ASP537 3.2 27.4 1.0
CG D:ASP535 3.3 28.4 1.0
OD2 D:ASP537 3.4 28.9 1.0
OD2 D:ASP535 3.5 32.7 1.0
NH2 D:ARG500 4.3 34.5 1.0
CB D:ASP539 4.5 27.4 1.0
CB D:ASP537 4.6 26.3 1.0
CB D:ASP535 4.6 28.5 1.0
N D:ASP537 4.8 29.1 1.0
N D:ASP535 4.9 27.7 1.0
N D:ASP539 4.9 24.2 1.0
C D:ASP537 4.9 25.8 1.0
O D:ASP537 5.0 24.2 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 Dec 14 21:16:02 2020

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