Magnesium in PDB 2fuc: Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound

All present enzymatic activity of Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound:
5.4.2.8;

The structure of Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound, PDB code: 2fuc was solved by N.R.Silvaggi, C.Zhang, Z.Lu, D.Dunaway-Mariano, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.33 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	51.690, 51.690, 215.980, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 20.6

The binding sites of Magnesium atom in the Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound (pdb code 2fuc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound, PDB code: 2fuc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:32.3 occ:1.00 O A:HOH1118 1.9 28.0 1.0 OD1 A:ASN218 2.1 29.0 1.0 O A:ASP21 2.1 30.4 1.0 O A:HOH1114 2.1 28.3 1.0 OD2 A:ASP19 2.1 26.9 1.0 O A:HOH1127 2.2 30.9 1.0 CG A:ASP19 3.0 27.2 1.0 CG A:ASN218 3.1 29.6 1.0 C A:ASP21 3.2 30.7 1.0 OD1 A:ASP19 3.3 27.0 1.0 ND2 A:ASN218 3.6 29.0 1.0 CA A:ASP21 4.0 30.4 1.0 OG1 A:THR23 4.1 29.0 1.0 CB A:ASP21 4.1 31.7 1.0 OD2 A:ASP226 4.1 29.1 1.0 N A:ASP21 4.1 29.9 1.0 OE2 A:GLU219 4.2 34.9 1.0 N A:GLY22 4.3 30.9 1.0 CB A:ASP19 4.4 27.6 1.0 CB A:ASN218 4.4 29.2 1.0 OD1 A:ASN225 4.4 32.9 1.0 CG A:GLU219 4.5 33.6 1.0 CD A:GLU219 4.6 35.0 1.0 CA A:GLY22 4.6 31.3 1.0 N A:THR23 4.6 30.9 1.0 N A:ASN218 4.6 28.0 1.0 C A:GLY22 4.8 31.8 1.0 C A:VAL20 4.8 28.6 1.0 O A:HOH1021 4.8 37.5 1.0 N A:GLU219 4.9 30.3 1.0 CA A:ASN218 4.9 29.2 1.0 CG A:ASP226 5.0 29.1 1.0 CB A:THR23 5.0 29.9 1.0 OD1 A:ASP226 5.0 28.2 1.0

Magnesium binding site 2 out of 2 in the Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Alpha-Phosphomannomutase 1 with MG2+ Cofactor Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:23.5 occ:1.00 O A:ASP232 2.2 26.5 1.0 O A:THR235 2.4 27.6 1.0 OG1 A:THR235 2.4 26.6 1.0 O A:PHE230 2.4 26.9 1.0 C A:THR235 3.2 26.7 1.0 C A:ASP232 3.3 27.0 1.0 C A:PHE230 3.4 27.8 1.0 CB A:THR235 3.5 26.5 1.0 C A:ALA231 3.6 27.9 1.0 N A:ASP232 3.6 27.5 1.0 CA A:THR235 3.7 26.5 1.0 N A:THR235 3.8 27.0 1.0 O A:ALA231 3.8 27.0 1.0 CA A:ASP232 4.0 27.7 1.0 O A:ILE229 4.1 27.7 1.0 CA A:ALA231 4.1 28.3 1.0 N A:GLY237 4.1 27.6 1.0 N A:ALA231 4.1 27.9 1.0 N A:VAL236 4.2 26.1 1.0 N A:PRO233 4.3 27.9 1.0 CA A:PRO233 4.5 27.6 1.0 C A:VAL236 4.5 28.1 1.0 CA A:PHE230 4.5 28.2 1.0 CA A:VAL236 4.5 26.3 1.0 CA A:GLY237 4.6 28.7 1.0 CG2 A:THR235 4.7 26.9 1.0 C A:PRO233 4.7 27.5 1.0 CB A:ASP232 4.8 28.5 1.0 N A:ARG234 4.8 26.9 1.0

N.R.Silvaggi, C.Zhang, Z.Lu, J.Dai, D.Dunaway-Mariano, K.N.Allen. The X-Ray Crystal Structures of Human Alpha-Phosphomannomutase 1 Reveal the Structural Basis of Congenital Disorder of Glycosylation Type 1A. J.Biol.Chem. V. 281 14918 2006.
ISSN: ISSN 0021-9258
PubMed: 16540464
DOI: 10.1074/JBC.M601505200