Magnesium in PDB 1wzc: Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate

All present enzymatic activity of Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate:
3.1.3.70;

The structure of Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate, PDB code: 1wzc was solved by T.Kawamura, N.Watanabe, I.Tanaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.833, 70.691, 67.911, 90.00, 98.15, 90.00
R / Rfree (%)	21.9 / 25.3

The binding sites of Magnesium atom in the Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate (pdb code 1wzc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate, PDB code: 1wzc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate


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 Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg300 b:22.5 occ:1.00 OD1 A:ASP8 1.9 21.2 1.0 O A:HOH439 2.0 23.6 1.0 OG A:SER169 2.0 24.7 1.0 O4 A:PO4401 2.1 21.8 1.0 O A:ASP10 2.1 23.3 1.0 OD2 A:ASP204 2.2 25.1 1.0 CG A:ASP8 3.0 27.2 1.0 CG A:ASP204 3.2 29.9 1.0 C A:ASP10 3.3 23.7 1.0 CB A:SER169 3.3 20.0 1.0 P A:PO4401 3.3 24.0 1.0 OD2 A:ASP8 3.4 26.0 1.0 OD1 A:ASP204 3.5 25.8 1.0 O1 A:PO4401 3.7 24.5 1.0 O3 A:PO4401 3.9 20.0 1.0 OG1 A:THR12 4.0 22.4 1.0 CA A:ASP10 4.0 24.0 1.0 N A:ASP10 4.1 22.7 1.0 CB A:ASP10 4.2 25.6 1.0 OD2 A:ASP208 4.2 24.0 1.0 O A:HOH442 4.2 31.5 1.0 CB A:ASP8 4.2 20.5 1.0 N A:LYS11 4.4 27.0 1.0 CA A:SER169 4.4 31.1 1.0 CB A:LYS11 4.4 30.7 1.0 O2 A:PO4401 4.5 24.2 1.0 N A:SER169 4.5 31.4 1.0 CB A:ASP204 4.6 22.0 1.0 C A:ILE9 4.7 24.6 1.0 N A:THR12 4.7 26.8 1.0 CB A:THR12 4.7 21.3 1.0 CA A:LYS11 4.8 27.4 1.0 N A:ILE9 4.8 20.7 1.0 C A:LYS11 4.8 28.4 1.0 OD1 A:ASN207 4.8 28.4 1.0 N A:ASP204 4.9 25.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Pyrococcus Horikoshii Mannosyl-3- Phosphoglycerate Phosphatase Complexed with MG2+ and Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:25.9 occ:1.00 OD1 B:ASP8 1.9 27.2 1.0 O4 B:PO4402 1.9 32.4 1.0 OG B:SER169 2.1 30.3 1.0 OD2 B:ASP204 2.1 30.8 1.0 O B:HOH438 2.2 30.1 1.0 O B:ASP10 2.2 31.7 1.0 CG B:ASP8 2.9 34.3 1.0 CG B:ASP204 3.1 36.1 1.0 P B:PO4402 3.3 32.5 1.0 C B:ASP10 3.3 32.4 1.0 CB B:SER169 3.3 25.1 1.0 OD2 B:ASP8 3.4 32.4 1.0 OD1 B:ASP204 3.5 36.1 1.0 O1 B:PO4402 3.7 31.1 1.0 O3 B:PO4402 3.9 31.6 1.0 CA B:ASP10 3.9 29.0 1.0 N B:ASP10 4.0 29.0 1.0 OG1 B:THR12 4.1 38.7 1.0 CB B:ASP10 4.1 32.8 1.0 OD2 B:ASP208 4.1 30.2 1.0 CB B:ASP8 4.3 27.1 1.0 O2 B:PO4402 4.4 25.7 1.0 N B:LYS11 4.4 34.9 1.0 O B:HOH421 4.5 31.6 1.0 CA B:SER169 4.5 32.0 1.0 CB B:ASP204 4.5 28.3 1.0 N B:SER169 4.6 31.6 1.0 CB B:LYS11 4.6 35.5 1.0 C B:ILE9 4.6 32.0 1.0 N B:THR12 4.7 29.3 1.0 C B:LYS11 4.8 33.1 1.0 N B:ILE9 4.8 32.8 1.0 CB B:THR12 4.8 36.2 1.0 CA B:LYS11 4.8 35.0 1.0 OD1 B:ASN207 4.8 36.0 1.0 N B:ASP204 4.9 33.2 1.0 NZ B:LYS180 5.0 26.8 1.0

T.Kawamura, N.Watanabe, I.Tanaka. Structure of Mannosyl-3-Phosphoglycerate Phosphatase From Pyrococcus Horikoshii. Acta Crystallogr.,Sect.D V. 64 1267 2008.
ISSN: ISSN 0907-4449
PubMed: 19018103
DOI: 10.1107/S0907444908033817