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Magnesium in PDB 6snp: Crystal Structures of Human PGM1 Isoform 2

Enzymatic activity of Crystal Structures of Human PGM1 Isoform 2

All present enzymatic activity of Crystal Structures of Human PGM1 Isoform 2:
5.4.2.2;

Protein crystallography data

The structure of Crystal Structures of Human PGM1 Isoform 2, PDB code: 6snp was solved by P.H.Backe, J.K.Laerdahl, L.S.Kittelsen, B.Dalhus, L.Morkrid, M.Bjoras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.47 / 2.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.339, 53.382, 76.066, 90.00, 100.15, 90.00
R / Rfree (%) 20.9 / 27

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structures of Human PGM1 Isoform 2 (pdb code 6snp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structures of Human PGM1 Isoform 2, PDB code: 6snp:

Magnesium binding site 1 out of 1 in 6snp

Go back to Magnesium Binding Sites List in 6snp
Magnesium binding site 1 out of 1 in the Crystal Structures of Human PGM1 Isoform 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structures of Human PGM1 Isoform 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:38.7
occ:1.00
OG A:SER135 2.0 45.0 1.0
OD1 A:ASP310 2.0 43.0 1.0
OD2 A:ASP306 2.2 47.0 1.0
OD1 A:ASP308 2.5 45.3 1.0
CG A:ASP310 2.8 42.8 1.0
OD2 A:ASP310 2.9 43.1 1.0
CB A:SER135 3.2 45.3 1.0
CG A:ASP306 3.3 45.4 1.0
CG A:ASP308 3.5 47.3 1.0
OD2 A:ASP308 3.6 48.9 1.0
CG A:ARG311 3.6 42.8 1.0
OD1 A:ASP306 3.8 44.7 1.0
CA A:SER135 3.9 46.8 1.0
NE A:ARG311 4.1 55.0 1.0
CB A:ASP310 4.2 36.8 1.0
CD A:ARG311 4.3 46.2 1.0
C A:SER135 4.4 46.2 1.0
CB A:ASP306 4.5 47.2 1.0
N A:HIS136 4.5 48.3 1.0
N A:ASP310 4.5 41.4 1.0
N A:ARG311 4.6 46.1 1.0
ND1 A:HIS136 4.7 51.0 1.0
CA A:ASP310 4.7 38.9 1.0
CZ A:ARG311 4.8 49.0 1.0
CB A:ASP308 4.8 49.0 1.0
C A:ASP310 4.9 45.3 1.0
CB A:ARG311 4.9 43.2 1.0
N A:ASP308 4.9 47.6 1.0

Reference:

P.H.Backe, J.K.Laerdahl, L.S.Kittelsen, B.Dalhus, L.Morkrid, M.Bjoras. Structural Basis For Substrate and Product Recognition in Human Phosphoglucomutase-1 (PGM1) Isoform 2, A Member of the Alpha-D-Phosphohexomutase Superfamily. Sci Rep V. 10 5656 2020.
ISSN: ESSN 2045-2322
PubMed: 32221390
DOI: 10.1038/S41598-020-62548-0
Page generated: Tue Oct 1 18:00:31 2024

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