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Magnesium in PDB 7epu: Crystal Structure of HSALC1

Enzymatic activity of Crystal Structure of HSALC1

All present enzymatic activity of Crystal Structure of HSALC1:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of HSALC1, PDB code: 7epu was solved by L.Wang, K.J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.40 / 3.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 153.48, 225.263, 106.533, 90, 90, 90
R / Rfree (%) 26.8 / 31.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of HSALC1 (pdb code 7epu). 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 Structure of HSALC1, PDB code: 7epu:

Magnesium binding site 1 out of 1 in 7epu

Go back to Magnesium Binding Sites List in 7epu
Magnesium binding site 1 out of 1 in the Crystal Structure of HSALC1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of HSALC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1202

b:69.8
occ:1.00
O1B B:ADP1201 2.3 124.4 1.0
OD2 B:ASP174 2.8 92.9 1.0
O3A B:ADP1201 3.0 102.5 1.0
OG1 B:THR78 3.1 132.6 1.0
PB B:ADP1201 3.2 143.1 1.0
OD1 B:ASP174 3.2 91.4 1.0
CG B:ASP174 3.4 78.5 1.0
O2B B:ADP1201 3.7 153.6 1.0
OE2 B:GLU175 4.1 127.0 1.0
CG B:LYS77 4.2 127.4 1.0
CD B:LYS77 4.3 117.8 1.0
NE1 B:TRP110 4.5 93.1 1.0
PA B:ADP1201 4.5 101.4 1.0
CB B:THR78 4.5 123.6 1.0
O3B B:ADP1201 4.5 81.8 1.0
O1A B:ADP1201 4.6 116.4 1.0
CZ2 B:TRP110 4.8 102.1 1.0
CG B:GLU175 4.8 143.0 1.0
CB B:ASP174 4.9 76.8 1.0
CE2 B:TRP110 4.9 98.5 1.0
N B:THR78 4.9 91.5 1.0
CD B:GLU175 4.9 158.1 1.0
CD2 B:LEU201 4.9 86.8 1.0

Reference:

L.Wang, K.Chen, Z.Chen. Structural Basis of ALC1/CHD1L Autoinhibition and the Mechanism of Activation By the Nucleosome. Nat Commun V. 12 4057 2021.
ISSN: ESSN 2041-1723
PubMed: 34210977
DOI: 10.1038/S41467-021-24320-4
Page generated: Thu Aug 14 07:04:50 2025

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