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Magnesium in PDB 1gsi: 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: 1gsi was solved by T.Ursby, M.Weik, E.Fioravanti, M.Delarue, M.Goeldner, D.Bourgeois, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.19 / 1.6
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.225, 76.225, 134.264, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 21

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 1gsi). 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: 1gsi:

Magnesium binding site 1 out of 1 in 1gsi

Go back to Magnesium Binding Sites List in 1gsi
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:Mg1209

b:14.4
occ:1.00
 OD1 A:ASP9 2.0 15.4 1.0
OE1 A:GLU166 2.0 19.1 1.0
O A:HOH2258 2.1 21.0 1.0
O A:HOH2200 2.1 16.3 1.0
O1P A:TMP1210 2.1 16.2 1.0
O A:HOH2207 2.1 18.8 1.0
CG A:ASP9 3.0 14.6 1.0
CD A:GLU166 3.1 19.1 1.0
P A:TMP1210 3.4 14.9 1.0
CG A:GLU166 3.7 16.7 1.0
CB A:ASP9 3.8 12.7 1.0
O3P A:TMP1210 3.8 15.2 1.0
O A:HOH2014 3.9 18.0 1.0
C3' A:TMP1210 4.0 13.9 1.0
OD2 A:ASP9 4.0 13.4 1.0
OE2 A:GLU166 4.0 17.7 1.0
O3' A:TMP1210 4.0 15.0 1.0
O5' A:TMP1210 4.1 13.7 1.0
O A:HOH2185 4.2 27.3 1.0
C5' A:TMP1210 4.2 14.6 1.0
O A:HOH2208 4.2 28.7 1.0
O A:HOH2087 4.2 33.1 1.0
OD2 A:ASP163 4.3 18.4 1.0
C4' A:TMP1210 4.5 15.6 1.0
O2P A:TMP1210 4.5 17.6 1.0
CA A:ASP9 4.6 12.8 1.0
O A:HOH2199 4.7 52.5 1.0
O A:HOH2209 4.7 41.4 1.0
O A:HOH2255 4.8 51.5 1.0

Reference:

T.Ursby, M.Weik, E.Fioravanti, M.Delarue, M.Goeldner, D.Bourgeois. Cryophotolysis of Caged Compounds: A Technique For Trapping Intermediate States in Protein Crystals Acta Crystallogr.,Sect.D V. 58 607 2002.
ISSN: ISSN 0907-4449
PubMed: 11914484
DOI: 10.1107/S0907444902002135
Page generated: Tue Aug 13 03:50:46 2024

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