Magnesium in PDB 8fg5: Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K

Enzymatic activity of Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K

All present enzymatic activity of Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K:
3.2.1.14;

Protein crystallography data

The structure of Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K, PDB code: 8fg5 was solved by R.E.Diaz, G.J.Correy, I.D.Young, M.C.Thompson, J.S.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.79 / 1.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.04, 42.25, 67.41, 90, 95.18, 90
R / Rfree (%) 13.2 / 15.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K (pdb code 8fg5). 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 Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K, PDB code: 8fg5:

Magnesium binding site 1 out of 1 in 8fg5

Go back to Magnesium Binding Sites List in 8fg5
Magnesium binding site 1 out of 1 in the Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Apo Mouse Acidic Mammalian Chitinase, Catalytic Domain at 100 K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:98.9
occ:1.00
O A:HOH769 2.1 33.0 1.0
O A:HOH762 2.6 21.8 1.0
OE1 A:GLN297 2.8 35.4 1.0
HE1 A:TRP31 3.0 21.8 1.0
O A:HOH641 3.1 31.2 1.0
HE22 A:GLN297 3.5 42.1 1.0
HZ2 A:TRP31 3.6 20.4 1.0
CD A:GLN297 3.6 33.9 1.0
NE1 A:TRP31 3.8 18.2 1.0
HH21 A:ARG35 3.9 22.5 1.0
NE2 A:GLN297 3.9 35.1 1.0
HZ A:PHE300 4.0 36.5 1.0
CZ A:PHE300 4.0 30.4 1.0
HH22 A:ARG35 4.1 22.5 1.0
CE2 A:PHE300 4.2 34.2 1.0
HE2 A:PHE300 4.3 41.0 1.0
CZ2 A:TRP31 4.3 17.0 1.0
NH2 A:ARG35 4.3 18.7 1.0
HE1 A:TRP360 4.4 18.9 1.0
CE2 A:TRP31 4.4 16.4 1.0
O A:HOH549 4.4 17.0 1.0
CE1 A:PHE300 4.5 34.5 1.0
HE21 A:GLN297 4.7 42.1 1.0
CD2 A:PHE300 4.8 44.5 1.0
HE1 A:PHE300 4.8 41.4 1.0
CD1 A:TRP31 4.9 17.6 1.0
HD21 A:LEU364 4.9 21.4 1.0
CG A:GLN297 4.9 30.9 1.0
HG3 A:GLN297 5.0 37.1 1.0

Reference:

R.E.Diaz, J.S.Fraser. Structural Characterization of Ligand Binding and pH-Specific Enzymatic Activity of Mouse Acidic Mammalian Chitinase To Be Published.
Page generated: Fri Apr 7 09:42:44 2023

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