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Magnesium in PDB 1tzf: X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi

Enzymatic activity of X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi

All present enzymatic activity of X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi:
2.7.7.33;

Protein crystallography data

The structure of X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi, PDB code: 1tzf was solved by N.M.Koropatkin, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.10
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 88.500, 88.500, 162.300, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi (pdb code 1tzf). 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 X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi, PDB code: 1tzf:

Magnesium binding site 1 out of 1 in 1tzf

Go back to Magnesium Binding Sites List in 1tzf
Magnesium binding site 1 out of 1 in the X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Crystal Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:21.2
occ:0.50
 O A:HOH664 1.9 10.1 0.5
O1A A:C5G401 1.9 30.1 1.0
O A:HOH663 1.9 9.1 0.5
O2B A:C5G401 2.1 56.4 1.0
OD2 A:ASP131 2.2 37.1 1.0
OD1 A:ASP236 2.4 49.5 1.0
PA A:C5G401 3.2 36.6 1.0
CG A:ASP131 3.2 36.1 1.0
PB A:C5G401 3.4 50.9 1.0
OD1 A:ASP131 3.5 26.7 1.0
CG A:ASP236 3.5 51.3 1.0
O3A A:C5G401 3.5 45.5 1.0
NZ A:LYS25 3.7 0.0 1.0
O6' A:C5G401 3.7 28.1 1.0
OD2 A:ASP236 3.8 43.3 1.0
C5D A:C5G401 4.0 42.1 1.0
O5' A:C5G401 4.1 25.3 1.0
O5D A:C5G401 4.1 40.4 1.0
O2A A:C5G401 4.2 31.4 1.0
O1B A:C5G401 4.3 37.6 1.0
CE A:LYS25 4.4 55.3 1.0
O1' A:C5G401 4.5 42.9 1.0
O A:HOH523 4.5 28.3 1.0
CB A:ASP131 4.5 24.4 1.0
C1' A:C5G401 4.7 14.8 1.0
C5' A:C5G401 4.7 19.9 1.0
CB A:PRO234 4.8 26.0 1.0
C6' A:C5G401 4.8 32.4 1.0
CB A:ASP236 4.8 36.3 1.0

Reference:

N.M.Koropatkin, H.M.Holden. Molecular Structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi J.Biol.Chem. V. 279 44023 2004.
ISSN: ISSN 0021-9258
PubMed: 15292268
DOI: 10.1074/JBC.M407755200
Page generated: Sun Aug 10 04:59:02 2025

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