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Magnesium in PDB 1mrs: Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with 5-CH2OH Deoxyuridine Monophosphate

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with 5-CH2OH Deoxyuridine Monophosphate

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with 5-CH2OH Deoxyuridine Monophosphate:
2.7.4.9;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with 5-CH2OH Deoxyuridine Monophosphate, PDB code: 1mrs was solved by A.Haouz, V.Vanheusden, H.Munier-Lehmann, M.Froeyen, P.Herdewijn, S.Van Calenbergh, M.Delarue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.400, 76.400, 134.400, 90.00, 90.00, 120.00
R / Rfree (%) 22.8 / 26.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with 5-CH2OH Deoxyuridine Monophosphate (pdb code 1mrs). 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 Complexed with 5-CH2OH Deoxyuridine Monophosphate, PDB code: 1mrs:

Magnesium binding site 1 out of 1 in 1mrs

Go back to Magnesium Binding Sites List in 1mrs
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with 5-CH2OH Deoxyuridine Monophosphate


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 Complexed with 5-CH2OH Deoxyuridine Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:47.0
occ:1.00
 O A:HOH317 2.0 33.9 1.0
OE2 A:GLU166 2.1 34.6 1.0
OP2 A:5HU217 2.1 38.8 1.0
OD1 A:ASP9 2.3 31.3 1.0
O A:HOH301 2.3 34.5 1.0
O A:HOH320 2.5 31.2 1.0
CD A:GLU166 3.1 34.4 1.0
CG A:ASP9 3.2 29.2 1.0
O5' A:5HU217 3.4 35.2 1.0
P A:5HU217 3.4 32.2 1.0
CG A:GLU166 3.8 33.0 1.0
CB A:ASP9 3.8 27.5 1.0
OE1 A:GLU166 3.9 35.3 1.0
OD2 A:ASP163 4.0 42.4 1.0
OD2 A:ASP9 4.0 26.2 1.0
O A:HOH352 4.1 49.2 1.0
O A:HOH316 4.1 35.0 1.0
C3' A:5HU217 4.2 33.4 1.0
OP3 A:5HU217 4.2 31.9 1.0
O3' A:5HU217 4.4 34.1 1.0
C5' A:5HU217 4.5 32.7 1.0
OP1 A:5HU217 4.6 34.0 1.0
C4' A:5HU217 4.7 33.0 1.0
CA A:ASP9 4.7 28.1 1.0
NH2 A:ARG95 4.9 25.6 1.0
CG A:ASP163 4.9 38.1 1.0

Reference:

A.Haouz, V.Vanheusden, H.Munier-Lehmann, M.Froeyen. Enzymatic and Structural Analysis of Inhibitors Designed Against Mycobacterium Tuberculosis Thymidylate Kinase. New Insights Into the Phosphoryl Transfer Mechanism. J.Biol.Chem. V. 278 4963 2003.
ISSN: ISSN 0021-9258
PubMed: 12454011
DOI: 10.1074/JBC.M209630200
Page generated: Tue Aug 13 09:11:45 2024

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