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Magnesium in PDB 1g3u: Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with Thymidine Monophosphate (Tmp)

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with Thymidine Monophosphate (Tmp)

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with Thymidine Monophosphate (Tmp):
2.7.4.9;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with Thymidine Monophosphate (Tmp), PDB code: 1g3u was solved by I.Li De La Sierra, H.Munier-Lehmann, A.M.Gilles, O.Barzu, M.Delarue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.95
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.622, 76.622, 134.378, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 25

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with Thymidine Monophosphate (Tmp) (pdb code 1g3u). 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 Thymidine Monophosphate (Tmp), PDB code: 1g3u:

Magnesium binding site 1 out of 1 in 1g3u

Go back to Magnesium Binding Sites List in 1g3u
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Thymidylate Kinase Complexed with Thymidine Monophosphate (Tmp)


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 Thymidine Monophosphate (Tmp) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg300

b:37.5
occ:1.00
 OD1 A:ASP9 2.3 20.2 1.0
OE2 A:GLU166 2.3 27.7 1.0
O A:HOH1009 2.3 25.6 1.0
O2P A:TMP217 2.3 32.6 1.0
O A:HOH1018 2.4 23.7 1.0
O A:HOH1050 2.4 35.1 1.0
CG A:ASP9 3.1 19.1 1.0
CD A:GLU166 3.2 25.8 1.0
P A:TMP217 3.5 33.1 1.0
CG A:GLU166 3.7 21.3 1.0
CB A:ASP9 3.7 17.5 1.0
O A:HOH1014 3.9 21.2 1.0
O3P A:TMP217 3.9 31.3 1.0
O A:HOH1071 3.9 42.7 1.0
OD2 A:ASP9 4.0 19.4 1.0
C3' A:TMP217 4.1 21.0 1.0
OE1 A:GLU166 4.1 27.2 1.0
O A:HOH1147 4.2 51.6 1.0
O3' A:TMP217 4.2 19.4 1.0
OD2 A:ASP163 4.4 23.6 1.0
O5' A:TMP217 4.4 27.4 1.0
C5' A:TMP217 4.4 24.9 1.0
CA A:ASP9 4.5 19.1 1.0
C4' A:TMP217 4.6 22.2 1.0
O1P A:TMP217 4.6 31.3 1.0
O A:HOH1119 4.6 54.6 1.0
NH2 A:ARG160 4.8 52.6 1.0

Reference:

I.Li De La Sierra, H.Munier-Lehmann, A.M.Gilles, O.Barzu, M.Delarue. X-Ray Structure of Tmp Kinase From Mycobacterium Tuberculosis Complexed with Tmp at 1.95 A Resolution. J.Mol.Biol. V. 311 87 2001.
ISSN: ISSN 0022-2836
PubMed: 11469859
DOI: 10.1006/JMBI.2001.4843
Page generated: Mon Dec 14 05:57:06 2020

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