Magnesium in PDB 6cfs: Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation M186Q

All present enzymatic activity of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation M186Q:
5.4.2.8;

The structure of Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation M186Q, PDB code: 6cfs 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)	41.40 / 2.07
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	50.890, 50.890, 213.600, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 23.6

The binding sites of Magnesium atom in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation M186Q (pdb code 6cfs). 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 M186Q, PDB code: 6cfs:
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 M186Q


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 M186Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:21.8 occ:1.00 O A:ASP21 2.0 19.8 1.0 O A:HOH457 2.0 18.7 1.0 O A:HOH468 2.0 20.6 1.0 OD2 A:ASP19 2.1 16.7 1.0 O A:HOH469 2.1 23.4 1.0 OD1 A:ASN218 2.2 20.4 1.0 CG A:ASP19 2.9 18.4 1.0 CG A:ASN218 3.2 19.6 1.0 OD1 A:ASP19 3.2 17.1 1.0 C A:ASP21 3.2 23.9 1.0 ND2 A:ASN218 3.6 20.3 1.0 CA A:ASP21 3.9 20.7 1.0 CB A:ASP21 4.0 23.3 1.0 OG1 A:THR23 4.0 19.6 1.0 N A:ASP21 4.1 20.2 1.0 OD2 A:ASP226 4.1 15.6 1.0 OE2 A:GLU219 4.2 22.2 1.0 N A:GLY22 4.3 22.1 1.0 O A:HOH627 4.3 24.1 1.0 CB A:ASP19 4.3 19.2 1.0 O A:HOH594 4.5 31.7 1.0 CA A:GLY22 4.5 20.2 1.0 CG A:GLU219 4.5 17.4 1.0 CB A:ASN218 4.5 22.4 1.0 OD1 A:ASN225 4.5 16.5 1.0 N A:ASN218 4.7 19.7 1.0 CD A:GLU219 4.7 21.2 1.0 N A:THR23 4.7 18.3 1.0 C A:VAL20 4.7 19.5 1.0 C A:GLY22 4.8 21.3 1.0 O A:HOH582 4.9 24.4 1.0 CG A:ASP226 4.9 17.8 1.0 CB A:THR23 4.9 18.8 1.0 OD1 A:ASP226 4.9 13.4 1.0 N A:GLU219 5.0 18.5 1.0

Magnesium binding site 2 out of 2 in the Structure of Human Alpha-Phosphomannomutase 1 Containing Mutation M186Q


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 M186Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:12.8 occ:1.00 O A:ASP232 2.2 13.7 1.0 O A:THR235 2.3 9.1 1.0 O A:PHE230 2.5 14.5 1.0 OG1 A:THR235 2.5 8.9 1.0 C A:THR235 3.1 14.1 1.0 C A:ASP232 3.3 13.1 1.0 C A:PHE230 3.5 15.9 1.0 C A:ALA231 3.6 18.0 1.0 CB A:THR235 3.6 11.5 1.0 N A:ASP232 3.7 14.5 1.0 CA A:THR235 3.7 9.9 1.0 N A:THR235 3.7 9.9 1.0 O A:ALA231 3.8 13.8 1.0 CA A:ASP232 4.0 11.9 1.0 O A:ILE229 4.1 11.9 1.0 N A:GLY237 4.1 10.1 1.0 CA A:ALA231 4.1 16.4 1.0 N A:ALA231 4.2 12.9 1.0 N A:VAL236 4.2 13.2 1.0 N A:PRO233 4.3 14.2 1.0 CA A:PRO233 4.5 13.7 1.0 C A:VAL236 4.5 14.7 1.0 CA A:VAL236 4.5 12.7 1.0 CA A:GLY237 4.5 12.3 1.0 CA A:PHE230 4.6 13.4 1.0 C A:PRO233 4.7 13.5 1.0 CG2 A:THR235 4.7 9.4 1.0 CB A:ASP232 4.7 14.5 1.0 N A:ARG234 4.8 13.7 1.0 C A:ARG234 5.0 11.9 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