Magnesium in PDB 6cfu: Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180K and R183K

All present enzymatic activity of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180K and R183K:
5.4.2.8;

The structure of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180K and R183K, PDB code: 6cfu 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)	49.28 / 2.24
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	50.650, 50.650, 213.410, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 27.4

The binding sites of Magnesium atom in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180K and R183K (pdb code 6cfu). 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 R180K and R183K, PDB code: 6cfu:
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 R180K and R183K


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 R180K and R183K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:36.2 occ:1.00 O A:ASP21 2.0 35.9 1.0 OD2 A:ASP19 2.0 27.4 1.0 OD1 A:ASN218 2.0 33.9 1.0 O A:HOH419 2.1 30.8 1.0 O A:HOH460 2.3 31.5 1.0 O A:HOH437 2.4 32.9 1.0 CG A:ASP19 2.9 26.8 1.0 CG A:ASN218 3.1 32.2 1.0 C A:ASP21 3.2 35.2 1.0 OD1 A:ASP19 3.3 27.9 1.0 ND2 A:ASN218 3.6 32.0 1.0 OD2 A:ASP226 3.9 30.1 1.0 OG1 A:THR23 3.9 32.0 1.0 CA A:ASP21 4.0 31.4 1.0 N A:ASP21 4.1 30.3 1.0 N A:GLY22 4.2 34.8 1.0 CB A:ASP21 4.2 36.3 1.0 CB A:ASP19 4.2 25.6 1.0 CB A:ASN218 4.3 32.4 1.0 CA A:GLY22 4.3 34.1 1.0 OE2 A:GLU219 4.3 34.3 1.0 N A:THR23 4.3 32.4 1.0 N A:ASN218 4.4 33.0 1.0 O A:HOH510 4.4 32.0 1.0 CG A:GLU219 4.4 28.6 1.0 C A:GLY22 4.6 35.5 1.0 OD1 A:ASN225 4.6 31.1 1.0 C A:VAL20 4.7 32.6 1.0 CG A:ASP226 4.7 27.8 1.0 CB A:THR23 4.7 28.1 1.0 OD1 A:ASP226 4.7 24.3 1.0 CD A:GLU219 4.7 33.8 1.0 CA A:ASN218 4.8 31.9 1.0 O A:HOH477 4.9 32.5 1.0 N A:GLU219 4.9 27.8 1.0 N A:VAL20 5.0 26.7 1.0 O A:VAL20 5.0 31.6 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutations R180K and R183K


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 R180K and R183K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:20.9 occ:1.00 O A:ASP232 2.2 19.2 1.0 O A:THR235 2.3 20.0 1.0 OG1 A:THR235 2.5 12.8 1.0 O A:PHE230 2.5 20.3 1.0 C A:THR235 3.1 19.5 1.0 C A:ASP232 3.3 22.6 1.0 C A:PHE230 3.5 25.3 1.0 CA A:THR235 3.6 18.2 1.0 N A:ASP232 3.6 20.8 1.0 C A:ALA231 3.6 24.9 1.0 CB A:THR235 3.6 16.7 1.0 N A:THR235 3.6 15.6 1.0 O A:ALA231 3.9 22.9 1.0 N A:GLY237 4.0 19.1 1.0 CA A:ASP232 4.0 21.9 1.0 O A:ILE229 4.0 22.9 1.0 N A:VAL236 4.1 19.4 1.0 CA A:ALA231 4.1 27.4 1.0 N A:ALA231 4.2 21.8 1.0 N A:PRO233 4.3 19.2 1.0 C A:VAL236 4.4 19.7 1.0 CA A:PRO233 4.4 22.3 1.0 CA A:GLY237 4.4 20.3 1.0 CA A:VAL236 4.5 17.7 1.0 CA A:PHE230 4.5 21.1 1.0 C A:PRO233 4.7 17.9 1.0 CG2 A:THR235 4.7 15.8 1.0 CB A:ASP232 4.7 22.6 1.0 N A:ARG234 4.8 19.1 1.0 C A:ARG234 4.9 16.4 1.0 C A:ILE229 5.0 22.5 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