Magnesium in PDB 6cft: Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I

All present enzymatic activity of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I:
5.4.2.8;

The structure of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I, PDB code: 6cft was solved by T.Ji, 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)	49.94 / 2.43
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	51.350, 51.350, 214.430, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 27.6

The binding sites of Magnesium atom in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I (pdb code 6cft). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I, PDB code: 6cft:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:42.0 occ:1.00 O A:HOH430 2.1 36.2 1.0 OD1 A:ASN218 2.2 38.5 1.0 O A:ASP21 2.2 37.2 1.0 OD2 A:ASP19 2.5 31.2 1.0 O A:HOH404 2.6 32.6 1.0 CG A:ASN218 3.2 38.0 1.0 CG A:ASP19 3.3 33.3 1.0 C A:ASP21 3.4 41.2 1.0 ND2 A:ASN218 3.4 35.8 1.0 OD1 A:ASP19 3.5 25.7 1.0 OE2 A:GLU219 3.8 41.2 1.0 CB A:ASP21 3.9 35.9 1.0 CA A:ASP21 4.0 38.5 1.0 CD A:GLU219 4.2 39.3 1.0 N A:ASP21 4.3 30.9 1.0 OD2 A:ASP226 4.3 38.6 1.0 CG A:GLU219 4.4 37.8 1.0 OG1 A:THR23 4.4 38.6 1.0 N A:GLY22 4.5 40.1 1.0 CB A:ASN218 4.6 43.8 1.0 OD1 A:ASN225 4.6 34.0 1.0 CB A:ASP19 4.6 33.1 1.0 CA A:GLY22 4.8 39.8 1.0 N A:ASN218 4.8 38.2 1.0 O A:HOH456 4.9 32.3 1.0 N A:THR23 4.9 42.6 1.0 N A:GLU219 4.9 33.9 1.0 CB A:GLU219 5.0 39.1 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180T and R183I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:23.6 occ:1.00 O A:ASP232 2.0 21.0 1.0 O A:THR235 2.2 23.2 1.0 O A:PHE230 2.6 24.1 1.0 OG1 A:THR235 2.7 22.6 1.0 C A:ASP232 3.1 22.5 1.0 C A:THR235 3.1 24.9 1.0 C A:ALA231 3.3 29.6 1.0 N A:ASP232 3.4 25.5 1.0 C A:PHE230 3.5 28.3 1.0 O A:ALA231 3.6 27.4 1.0 CA A:THR235 3.6 21.6 1.0 N A:THR235 3.6 21.0 1.0 CB A:THR235 3.7 22.7 1.0 CA A:ASP232 3.8 24.1 1.0 CA A:ALA231 3.9 31.8 1.0 N A:ALA231 4.0 26.2 1.0 O A:ILE229 4.1 27.0 1.0 N A:GLY237 4.1 22.0 1.0 N A:PRO233 4.1 21.9 1.0 N A:VAL236 4.2 21.5 1.0 CA A:PRO233 4.4 23.5 1.0 CB A:ASP232 4.5 23.6 1.0 CA A:PHE230 4.6 28.7 1.0 CA A:VAL236 4.6 20.0 1.0 C A:PRO233 4.6 26.0 1.0 C A:VAL236 4.6 24.5 1.0 N A:ARG234 4.7 26.5 1.0 CA A:GLY237 4.7 27.2 1.0 CG2 A:THR235 4.8 19.5 1.0 C A:ARG234 4.9 22.0 1.0 C A:ILE229 5.0 28.2 1.0

T.Ji, C.Zhang, L.Zheng, D.Dunaway-Mariano, K.N.Allen. Structural Basis of the Molecular Switch Between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 Under Ischemic Conditions. Biochemistry V. 57 3480 2018.
ISSN: ISSN 1520-4995
PubMed: 29695157
DOI: 10.1021/ACS.BIOCHEM.8B00223