Magnesium in PDB 6cfv: Structure of Human Alpha-Phosphomannomutase 1 in Complex with Inosine Monophosphate

All present enzymatic activity of Structure of Human Alpha-Phosphomannomutase 1 in Complex with Inosine Monophosphate:
5.4.2.8;

The structure of Structure of Human Alpha-Phosphomannomutase 1 in Complex with Inosine Monophosphate, PDB code: 6cfv 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)	34.88 / 1.92
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	52.169, 52.169, 214.484, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 22.6

The binding sites of Magnesium atom in the Structure of Human Alpha-Phosphomannomutase 1 in Complex with Inosine Monophosphate (pdb code 6cfv). 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 in Complex with Inosine Monophosphate, PDB code: 6cfv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 in Complex with Inosine Monophosphate


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 in Complex with Inosine Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:25.1 occ:1.00 O A:HOH440 2.1 21.9 1.0 O A:ASP21 2.1 24.6 1.0 OD2 A:ASP19 2.1 20.9 1.0 OD1 A:ASN218 2.1 23.7 1.0 O A:HOH421 2.2 23.2 1.0 O A:HOH444 2.2 23.0 1.0 CG A:ASP19 3.0 19.7 1.0 CG A:ASN218 3.2 23.9 1.0 C A:ASP21 3.3 26.0 1.0 OD1 A:ASP19 3.3 19.5 1.0 ND2 A:ASN218 3.7 23.9 1.0 CA A:ASP21 4.0 24.8 1.0 CB A:ASP21 4.0 25.3 1.0 OD2 A:ASP226 4.1 23.2 1.0 O A:HOH538 4.1 32.0 1.0 N A:ASP21 4.1 22.3 1.0 OG1 A:THR23 4.1 19.1 1.0 O A:HOH633 4.2 33.0 1.0 OE2 A:GLU219 4.3 27.0 1.0 N A:GLY22 4.3 25.2 1.0 CB A:ASP19 4.4 19.3 1.0 OD1 A:ASN225 4.5 21.9 1.0 CB A:ASN218 4.5 25.1 1.0 CG A:GLU219 4.5 26.7 1.0 N A:ASN218 4.6 21.3 1.0 CA A:GLY22 4.6 25.1 1.0 N A:THR23 4.7 24.5 1.0 CD A:GLU219 4.7 30.9 1.0 C A:VAL20 4.8 21.1 1.0 O A:HOH566 4.8 26.4 1.0 C A:GLY22 4.8 25.2 1.0 CG A:ASP226 4.9 19.6 1.0 N A:GLU219 4.9 22.5 1.0 OD1 A:ASP226 5.0 19.6 1.0 CA A:ASN218 5.0 21.2 1.0 CB A:THR23 5.0 23.3 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 in Complex with Inosine Monophosphate


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 in Complex with Inosine Monophosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:17.6 occ:1.00 O A:ASP232 2.3 17.6 1.0 O A:THR235 2.3 16.4 1.0 O A:PHE230 2.4 16.8 1.0 OG1 A:THR235 2.4 17.6 1.0 C A:THR235 3.1 17.1 1.0 C A:ASP232 3.4 19.7 1.0 C A:PHE230 3.4 17.5 1.0 CB A:THR235 3.6 14.8 1.0 C A:ALA231 3.6 23.7 1.0 N A:ASP232 3.6 16.4 1.0 CA A:THR235 3.7 14.7 1.0 N A:THR235 3.8 15.1 1.0 O A:ALA231 3.9 20.6 1.0 N A:GLY237 4.0 19.1 1.0 CA A:ASP232 4.0 20.7 1.0 CA A:ALA231 4.0 23.3 1.0 O A:ILE229 4.1 17.4 1.0 N A:ALA231 4.1 17.2 1.0 N A:VAL236 4.2 13.9 1.0 N A:PRO233 4.4 20.8 1.0 C A:VAL236 4.4 21.6 1.0 CA A:VAL236 4.5 17.6 1.0 CA A:GLY237 4.5 20.3 1.0 CA A:PHE230 4.5 17.4 1.0 CA A:PRO233 4.5 19.9 1.0 CG2 A:THR235 4.7 15.8 1.0 CB A:ASP232 4.8 21.3 1.0 C A:PRO233 4.8 20.4 1.0 N A:ARG234 5.0 19.3 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