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Magnesium in PDB 1n5k: Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A)

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A)

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A):
2.7.4.9;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A), PDB code: 1n5k was solved by E.Fioravanti, A.Haouz, T.Ursby, H.Munier-Lehmann, M.Delarue, D.Bourgeois, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.71 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 64.254, 64.254, 195.484, 90.00, 90.00, 120.00
R / Rfree (%) 21.5 / 24.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A) (pdb code 1n5k). 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 Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A), PDB code: 1n5k:

Magnesium binding site 1 out of 1 in 1n5k

Go back to Magnesium Binding Sites List in 1n5k
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A)


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 Thymidylate Kinase Crystallized in Sodium Malonate (Resolution 2.1 A) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg413

b:45.7
occ:1.00
 O3P B:TMP411 1.8 36.3 1.0
O B:HOH513 2.0 53.6 1.0
OD1 B:ASP9 2.2 29.1 1.0
O B:HOH471 2.6 56.8 1.0
CG B:ASP9 3.3 28.6 1.0
P B:TMP411 3.4 32.1 1.0
O B:HOH474 3.4 55.8 1.0
O B:HOH470 3.6 38.0 1.0
CB B:ASP9 3.7 28.0 1.0
O2P B:TMP411 4.1 35.8 1.0
CA B:ASP9 4.1 26.4 1.0
OE1 B:GLU166 4.1 44.4 1.0
NH1 B:ARG95 4.1 24.1 1.0
O1P B:TMP411 4.2 34.2 1.0
OD2 B:ASP9 4.3 28.9 1.0
O5' B:TMP411 4.5 31.8 1.0
C3' B:TMP411 4.5 29.0 1.0
O3' B:TMP411 4.7 25.8 1.0
CD B:GLU166 4.9 42.9 1.0
NE B:ARG95 4.9 27.6 1.0
CG B:GLU166 4.9 38.6 1.0
N B:GLY10 5.0 26.6 1.0

Reference:

E.Fioravanti, A.Haouz, T.Ursby, H.Munier-Lehmann, M.Delarue, D.Bourgeois. Mycobacterium Tuberculosis Thymidylate Kinase: Structural Studies of Intermediates Along the Reaction Pathway J.Mol.Biol. V. 375 1077 2003.
ISSN: ISSN 0022-2836
PubMed: 12662932
DOI: 10.1016/S0022-2836(03)00202-X
Page generated: Tue Aug 13 09:22:30 2024

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