Magnesium in PDB 8j2f: Human Neutral Shpingomyelinase

Enzymatic activity of Human Neutral Shpingomyelinase

All present enzymatic activity of Human Neutral Shpingomyelinase:
3.1.4.12;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Neutral Shpingomyelinase (pdb code 8j2f). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Neutral Shpingomyelinase, PDB code: 8j2f:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8j2f

Go back to Magnesium Binding Sites List in 8j2f
Magnesium binding site 1 out of 2 in the Human Neutral Shpingomyelinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Neutral Shpingomyelinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:30.0
occ:1.00
OE2 A:GLU49 2.5 55.8 1.0
OE1 A:GLU49 2.8 55.8 1.0
CD A:GLU49 3.0 55.8 1.0
CD1 A:TRP17 4.2 72.6 1.0
OD2 A:ASP271 4.2 76.2 1.0
NE2 A:HIS272 4.4 68.9 1.0
ND2 A:ASN15 4.4 59.0 1.0
CG A:GLU49 4.5 55.8 1.0
CD2 A:HIS272 4.7 68.9 1.0
OD1 A:ASP271 5.0 76.2 1.0

Magnesium binding site 2 out of 2 in 8j2f

Go back to Magnesium Binding Sites List in 8j2f
Magnesium binding site 2 out of 2 in the Human Neutral Shpingomyelinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Neutral Shpingomyelinase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:30.0
occ:1.00
OE2 B:GLU49 2.5 55.8 1.0
OE1 B:GLU49 2.8 55.8 1.0
CD B:GLU49 3.0 55.8 1.0
CD1 B:TRP17 4.2 72.6 1.0
OD2 B:ASP271 4.2 76.2 1.0
NE2 B:HIS272 4.4 68.9 1.0
ND2 B:ASN15 4.4 59.0 1.0
CG B:GLU49 4.5 55.8 1.0
CD2 B:HIS272 4.7 68.9 1.0
OD1 B:ASP271 5.0 76.2 1.0

Reference:

J.Yi, B.Qi, J.Yin, R.Li, X.Chen, J.Hu, G.Li, S.Zhang, Y.Zhang, M.Yang. Molecular Basis For the Catalytic Mechanism of Human Neutral Sphingomyelinases 1 (HSMPD2) Nat Commun V. 14 7755 2023.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-023-43580-W
Page generated: Fri Oct 4 11:29:52 2024

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