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Magnesium in PDB 7ckp: Mycobacterium Tuberculosis Enolase

Enzymatic activity of Mycobacterium Tuberculosis Enolase

All present enzymatic activity of Mycobacterium Tuberculosis Enolase:
4.2.1.11;

Protein crystallography data

The structure of Mycobacterium Tuberculosis Enolase, PDB code: 7ckp was solved by B.K.Biswal, M.Ahmad, B.Jha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.92 / 2.90
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 141.062, 141.062, 95.536, 90, 90, 90
R / Rfree (%) 24.3 / 29.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mycobacterium Tuberculosis Enolase (pdb code 7ckp). 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 Enolase, PDB code: 7ckp:

Magnesium binding site 1 out of 1 in 7ckp

Go back to Magnesium Binding Sites List in 7ckp
Magnesium binding site 1 out of 1 in the Mycobacterium Tuberculosis Enolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Tuberculosis Enolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:78.8
occ:1.00
OD2 A:ASP241 1.9 60.4 1.0
OD2 A:ASP310 2.2 67.0 1.0
CG A:ASP241 3.0 62.9 1.0
CG A:ASP310 3.5 71.7 1.0
CD A:GLN162 3.6 91.6 1.0
OE2 A:GLU283 3.7 81.5 1.0
OD1 A:ASP241 3.7 59.7 1.0
O4 A:MPD502 3.8 82.0 1.0
OD1 A:ASP311 4.1 100.6 1.0
CB A:ASP241 4.1 65.6 1.0
NZ A:LYS386 4.2 68.6 1.0
OD1 A:ASP310 4.2 67.6 1.0
OE2 A:GLU163 4.3 77.8 1.0
CD A:GLU283 4.4 83.0 1.0
CB A:ASP310 4.4 75.4 1.0
CD A:GLU163 4.7 77.7 1.0
O2 A:MPD502 4.8 89.4 1.0
NZ A:LYS335 4.8 95.4 1.0
OE1 A:GLU283 4.9 84.8 1.0
OD2 A:ASP284 4.9 102.8 1.0
C4 A:MPD502 5.0 81.6 1.0
CA A:ALA243 5.0 75.4 1.0
C5 A:MPD502 5.0 79.1 1.0
CG A:GLN162 5.0 90.3 1.0

Reference:

B.K.Biswal, M.Ahmad, B.Jha. Mycobacterium Tuberculosis Enolase To Be Published.
Page generated: Wed Oct 2 14:11:42 2024

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