Magnesium in PDB 6cfr: Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation R183I

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

The structure of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation R183I, PDB code: 6cfr 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)	42.11 / 2.07
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	51.910, 51.910, 216.080, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 21.2

The binding sites of Magnesium atom in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation R183I (pdb code 6cfr). 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 Mutation R183I, PDB code: 6cfr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation 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 Mutation R183I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:13.2 occ:1.00 O A:HOH435 2.1 8.8 1.0 O A:HOH427 2.1 12.1 1.0 O A:ASP21 2.1 11.9 1.0 OD1 A:ASN218 2.1 7.9 1.0 O A:HOH486 2.1 9.3 1.0 OD2 A:ASP19 2.2 8.0 1.0 CG A:ASP19 3.1 8.2 1.0 CG A:ASN218 3.1 8.1 1.0 C A:ASP21 3.3 12.3 1.0 OD1 A:ASP19 3.4 6.7 1.0 ND2 A:ASN218 3.5 10.5 1.0 OG1 A:THR23 4.0 7.5 1.0 OD2 A:ASP226 4.0 7.7 1.0 CA A:ASP21 4.1 8.2 1.0 OE2 A:GLU219 4.2 13.6 1.0 CB A:ASP21 4.2 9.7 1.0 O A:HOH676 4.2 19.5 1.0 N A:ASP21 4.3 5.4 1.0 O A:HOH655 4.3 24.6 1.0 N A:GLY22 4.3 11.3 1.0 OD1 A:ASN225 4.4 9.1 1.0 CG A:GLU219 4.4 15.4 1.0 CB A:ASP19 4.5 10.4 1.0 CB A:ASN218 4.5 7.8 1.0 CA A:GLY22 4.5 10.9 1.0 CD A:GLU219 4.5 12.1 1.0 N A:ASN218 4.6 7.8 1.0 N A:THR23 4.7 10.8 1.0 C A:GLY22 4.8 12.5 1.0 N A:GLU219 4.8 8.2 1.0 O A:HOH528 4.8 12.2 1.0 CG A:ASP226 4.9 8.5 1.0 OD1 A:ASP226 4.9 5.5 1.0 CA A:ASN218 4.9 9.5 1.0 C A:VAL20 5.0 7.7 1.0 CB A:THR23 5.0 8.7 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation 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 Mutation R183I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:10.7 occ:1.00 O A:ASP232 2.2 6.8 1.0 O A:PHE230 2.4 5.9 1.0 O A:THR235 2.4 8.7 1.0 OG1 A:THR235 2.4 6.8 1.0 C A:THR235 3.2 9.2 1.0 C A:ASP232 3.4 8.5 1.0 C A:PHE230 3.4 9.0 1.0 C A:ALA231 3.6 13.1 1.0 CB A:THR235 3.6 7.4 1.0 N A:ASP232 3.6 8.8 1.0 CA A:THR235 3.7 7.3 1.0 N A:THR235 3.8 9.0 1.0 O A:ALA231 3.9 7.3 1.0 O A:ILE229 4.0 5.6 1.0 N A:GLY237 4.0 7.7 1.0 CA A:ALA231 4.0 12.1 1.0 N A:ALA231 4.1 8.9 1.0 CA A:ASP232 4.1 7.2 1.0 N A:VAL236 4.2 7.7 1.0 N A:PRO233 4.4 8.0 1.0 CA A:PHE230 4.4 7.3 1.0 C A:VAL236 4.5 9.6 1.0 CA A:VAL236 4.5 6.2 1.0 CA A:GLY237 4.5 8.3 1.0 CA A:PRO233 4.6 9.3 1.0 CG2 A:THR235 4.6 8.6 1.0 C A:PRO233 4.8 8.4 1.0 CB A:ASP232 4.8 9.4 1.0 C A:ILE229 4.9 6.2 1.0 N A:ARG234 5.0 10.4 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