Magnesium in PDB 1wvc: Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp

All present enzymatic activity of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp:
2.7.7.33;

The structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp, PDB code: 1wvc was solved by N.M.Koropatkin, W.W.Cleland, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.50
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	84.200, 84.200, 157.400, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The structure of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Magnesium atom in the Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp (pdb code 1wvc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp, PDB code: 1wvc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:36.6 occ:1.00 OD2 A:ASP131 2.0 42.1 1.0 OD1 A:ASP236 2.1 44.2 1.0 O2A A:CTP401 2.5 0.0 1.0 CG A:ASP236 3.0 39.6 1.0 CG A:ASP131 3.0 40.2 1.0 O1A A:CTP401 3.1 33.7 1.0 OD2 A:ASP236 3.2 40.4 1.0 PA A:CTP401 3.3 32.6 1.0 OD1 A:ASP131 3.3 38.5 1.0 NH2 A:ARG15 3.6 72.4 1.0 O A:HOH713 3.8 40.8 1.0 NZ A:LYS25 4.0 50.0 1.0 C5' A:CTP401 4.1 54.2 1.0 O5' A:CTP401 4.2 42.1 1.0 O A:HOH2515 4.3 83.7 1.0 CB A:ASP131 4.3 35.6 1.0 CB A:ASP236 4.4 21.4 1.0 CZ A:ARG15 4.4 82.0 1.0 NH1 A:ARG15 4.6 52.0 1.0 O A:HOH1902 4.7 68.3 1.0 O3A A:CTP401 4.8 53.7 1.0 CB A:PRO234 4.9 34.3 1.0 CE A:LYS25 4.9 17.4 1.0 O A:HOH1905 5.0 20.9 1.0

Magnesium binding site 2 out of 2 in the Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase Complexed with Ctp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:54.2 occ:1.00 O3A A:CTP401 2.4 53.7 1.0 O1G A:CTP401 2.8 37.9 1.0 PA A:CTP401 3.4 32.6 1.0 O2A A:CTP401 3.4 0.0 1.0 PB A:CTP401 3.5 35.2 1.0 O A:HOH2515 3.6 83.7 1.0 O1B A:CTP401 3.6 37.5 1.0 O5' A:CTP401 3.8 42.1 1.0 NH2 A:ARG15 3.9 72.4 1.0 PG A:CTP401 4.0 44.5 1.0 O3B A:CTP401 4.1 45.4 1.0 O A:HOH1907 4.5 50.8 1.0 O1A A:CTP401 4.6 33.7 1.0 O2B A:CTP401 4.7 68.2 1.0 O2G A:CTP401 4.7 42.9 1.0 C6 A:CTP401 4.8 20.7 1.0 C5 A:CTP401 4.8 30.9 1.0 CZ A:ARG15 4.9 82.0 1.0

N.M.Koropatkin, W.W.Cleland, H.M.Holden. Kinetic and Structural Analysis of Alpha-D-Glucose-1-Phosphate Cytidylyltransferase From Salmonella Typhi. J.Biol.Chem. V. 280 10774 2005.
ISSN: ISSN 0021-9258
PubMed: 15634670
DOI: 10.1074/JBC.M414111200