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Magnesium in PDB 1lvh: The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution

Enzymatic activity of The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution

All present enzymatic activity of The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution:
5.4.2.6;

Protein crystallography data

The structure of The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution, PDB code: 1lvh was solved by S.D.Lahiri, G.Zhang, 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) 42.89 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.667, 92.776, 111.597, 90.00, 90.00, 90.00
R / Rfree (%) 24.4 / 28.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution (pdb code 1lvh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution, PDB code: 1lvh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1lvh

Go back to Magnesium Binding Sites List in 1lvh
Magnesium binding site 1 out of 2 in the The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg801

b:1.0
occ:1.00
OD1 A:ASP170 1.8 18.0 1.0
OD2 A:PHD8 2.0 15.0 1.0
O A:ASP10 2.0 16.8 1.0
OP3 A:PHD8 2.3 22.2 1.0
CG A:ASP170 2.8 20.3 1.0
CG A:PHD8 3.0 14.1 1.0
OD2 A:ASP170 3.2 22.1 1.0
C A:ASP10 3.2 16.9 1.0
P A:PHD8 3.4 25.7 1.0
OD1 A:PHD8 3.4 18.4 1.0
OE1 A:GLU169 3.9 19.7 1.0
O A:HOH866 3.9 30.8 1.0
CB A:ASP10 4.0 19.3 1.0
CA A:ASP10 4.0 18.1 1.0
OD2 A:ASP10 4.0 25.0 1.0
OP2 A:PHD8 4.1 21.4 1.0
CB A:ASP170 4.2 20.2 1.0
N A:GLY11 4.2 14.9 1.0
N A:ASP10 4.3 19.6 1.0
CB A:PHD8 4.3 18.6 1.0
O A:HOH951 4.4 30.8 1.0
CG A:ASP10 4.4 22.3 1.0
CA A:GLY11 4.5 18.6 1.0
OP1 A:PHD8 4.5 21.5 1.0
N A:ASP170 4.5 17.1 1.0
CD A:GLU169 4.7 19.9 1.0
CA A:ASP170 4.8 18.2 1.0
N A:SER171 4.8 18.0 1.0
OE2 A:GLU169 4.9 20.7 1.0
CB A:SER171 4.9 21.4 1.0
C A:ASP170 4.9 19.2 1.0

Magnesium binding site 2 out of 2 in 1lvh

Go back to Magnesium Binding Sites List in 1lvh
Magnesium binding site 2 out of 2 in the The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis to 2.3 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg800

b:1.0
occ:1.00
OD2 B:PHD8 1.9 25.7 1.0
O B:ASP10 1.9 32.9 1.0
OD1 B:ASP170 1.9 17.5 1.0
OP1 B:PHD8 2.1 31.1 1.0
CG B:ASP170 2.9 20.9 1.0
CG B:PHD8 2.9 26.0 1.0
OE1 B:GLU169 3.0 31.4 1.0
C B:ASP10 3.1 31.8 1.0
P B:PHD8 3.2 33.4 1.0
OD2 B:ASP170 3.3 20.6 1.0
OD1 B:PHD8 3.3 30.5 1.0
CA B:ASP10 3.9 33.6 1.0
CB B:ASP10 4.0 34.9 1.0
CD B:GLU169 4.1 28.1 1.0
OP3 B:PHD8 4.1 28.7 1.0
N B:GLY11 4.2 30.0 1.0
N B:ASP10 4.2 34.0 1.0
CB B:ASP170 4.3 21.7 1.0
CB B:PHD8 4.3 27.3 1.0
OP2 B:PHD8 4.3 31.0 1.0
CA B:GLY11 4.4 27.2 1.0
N B:ASP170 4.4 22.3 1.0
OD2 B:ASP10 4.5 38.9 1.0
OE2 B:GLU169 4.7 23.3 1.0
CG B:ASP10 4.8 36.8 1.0
N B:SER171 4.8 25.4 1.0
CA B:ASP170 4.8 24.1 1.0
OG B:SER171 4.9 27.8 1.0
C B:LEU9 4.9 35.9 1.0
CG B:GLU169 5.0 28.4 1.0

Reference:

S.D.Lahiri, G.Zhang, D.Dunaway-Mariano, K.N.Allen. Caught in the Act: the Structure of Phosphorylated Beta-Phosphoglucomutase From Lactococcus Lactis. Biochemistry V. 41 8351 2002.
ISSN: ISSN 0006-2960
PubMed: 12081483
DOI: 10.1021/BI0202373
Page generated: Mon Dec 14 06:23:41 2020

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