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Zinc in PDB 6snq: 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: 6snq 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) 48.63 / 2.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 73.262, 53.155, 76.825, 90.00, 99.14, 90.00
R / Rfree (%) 20.6 / 24.6

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 6snq

Go back to Zinc Binding Sites List in 6snq
Zinc 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 Zinc with other atoms in the Zn binding site number 1 of Crystal Structures of Human PGM1 Isoform 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:45.4
occ:1.00
OD2 A:ASP306 2.0 38.8 1.0
OD1 A:ASP310 2.0 42.9 1.0
OD1 A:ASP308 2.2 39.0 1.0
OG A:SEP135 2.4 58.8 1.0
O2P A:SEP135 2.7 56.5 1.0
P A:SEP135 2.8 77.8 1.0
CG A:ASP310 2.9 40.7 1.0
CG A:ASP308 3.0 39.2 1.0
OD2 A:ASP310 3.1 40.9 1.0
O3P A:SEP135 3.1 65.0 1.0
CG A:ASP306 3.2 39.7 1.0
OD2 A:ASP308 3.2 36.2 1.0
CB A:SEP135 3.5 50.9 1.0
OD1 A:ASP306 3.7 41.2 1.0
CA A:SEP135 3.8 43.0 1.0
CD A:ARG311 3.9 39.7 1.0
CG A:ARG311 4.1 40.3 1.0
CB A:ASP310 4.3 37.5 1.0
C A:SEP135 4.3 45.8 1.0
O1P A:SEP135 4.4 58.0 1.0
N A:ASP310 4.4 34.6 1.0
CB A:ASP306 4.4 40.7 1.0
NE A:ARG311 4.4 45.2 1.0
N A:HIS136 4.4 47.6 1.0
CB A:ASP308 4.4 37.1 1.0
N A:ASP308 4.6 38.3 1.0
CA A:ASP310 4.7 35.0 1.0
N A:GLY309 4.8 37.9 1.0
N A:ARG311 4.8 38.0 1.0
C A:ASP310 4.9 36.8 1.0
CA A:ASP308 4.9 35.2 1.0
CB A:ARG311 5.0 37.5 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 29 07:31:25 2024

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