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Magnesium in PDB 7ev3: Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp:
6.1.1.2;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp, PDB code: 7ev3 was solved by M.Xu, S.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.89 / 2.70
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.266, 61.266, 333.627, 90, 90, 120
R / Rfree (%) 20.1 / 24.9

Other elements in 7ev3:

The structure of Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp also contains other interesting chemical elements:

Fluorine (F) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp (pdb code 7ev3). 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 Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp, PDB code: 7ev3:

Magnesium binding site 1 out of 1 in 7ev3

Go back to Magnesium Binding Sites List in 7ev3
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp


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 Tryptophanyl-Trna Synthetase Complexed with Y-10 and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:38.3
occ:1.00
 O2A A:ATP401 2.2 39.2 1.0
O2G A:ATP401 2.2 54.7 1.0
O A:HOH517 2.2 43.4 1.0
O2B A:ATP401 2.2 52.6 1.0
O A:HOH501 2.2 48.2 1.0
PB A:ATP401 3.4 49.7 1.0
O1 A:JE3403 3.5 39.1 1.0
PG A:ATP401 3.5 59.1 1.0
PA A:ATP401 3.5 41.9 1.0
O3B A:ATP401 3.7 45.4 1.0
O3A A:ATP401 3.9 43.2 1.0
NE2 A:GLN15 4.0 31.5 1.0
O1G A:ATP401 4.1 58.0 1.0
O5' A:ATP401 4.2 43.6 1.0
C5 A:JE3403 4.2 37.8 1.0
OD2 A:ASP155 4.2 48.7 1.0
N1 A:JE3403 4.3 37.9 1.0
O A:HOH544 4.4 44.0 1.0
NZ A:LYS201 4.5 53.6 1.0
NE2 A:GLN156 4.6 47.0 1.0
O3G A:ATP401 4.7 43.1 1.0
O1B A:ATP401 4.7 53.7 1.0
O1A A:ATP401 4.8 30.8 1.0

Reference:

Y.Yang, Y.Xu, Y.Yue, H.Wang, Y.Cui, M.Pan, X.Zhang, L.Zhang, H.Li, M.Xu, Y.Tang, S.Chen. Investigate Natural Product Indolmycin and the Synthetically Improved Analogue Toward Antimycobacterial Agents. Acs Chem.Biol. V. 17 39 2022.
ISSN: ESSN 1554-8937
PubMed: 34908399
DOI: 10.1021/ACSCHEMBIO.1C00394
Page generated: Wed Oct 2 21:03:03 2024

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