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Magnesium in PDB 8oo9: Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1

Other elements in 8oo9:

The structure of Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1 also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Aluminium (Al) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1 (pdb code 8oo9). 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 Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1, PDB code: 8oo9:

Magnesium binding site 1 out of 1 in 8oo9

Go back to Magnesium Binding Sites List in 8oo9
Magnesium binding site 1 out of 1 in the Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1 within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg2002

b:64.3
occ:1.00
F3 G:ALF2003 1.9 62.5 1.0
O2B G:ADP2001 2.0 58.6 1.0
PB G:ADP2001 3.2 39.9 1.0
OG1 G:THR1004 3.3 46.5 1.0
AL G:ALF2003 3.5 61.9 1.0
O1B G:ADP2001 3.5 51.9 1.0
F2 G:ALF2003 3.6 70.9 1.0
OE2 G:GLU1108 3.8 69.7 1.0
O1A G:ADP2001 4.1 58.6 1.0
O3B G:ADP2001 4.2 52.6 1.0
F1 G:ALF2003 4.3 51.9 1.0
O3A G:ADP2001 4.3 57.6 1.0
CZ3 G:TRP1036 4.3 62.4 1.0
PA G:ADP2001 4.5 55.5 1.0
O2A G:ADP2001 4.5 54.6 1.0
CA G:GLY1634 4.7 57.1 1.0
CB G:THR1004 4.7 48.5 1.0
CE3 G:TRP1036 4.7 56.3 1.0
O G:GLY1634 4.8 58.6 1.0
N G:THR1004 4.9 45.2 1.0
NH2 G:ARG1664 4.9 60.2 1.0
CD G:GLU1108 5.0 71.3 1.0

Reference:

M.Zhang, A.Jungblut, F.Kunert, L.Hauptmann, T.Hoffmann, O.Kolesnikova, F.Metzner, M.Moldt, F.Weis, F.Dimaio, K.P.Hopfner, S.Eustermann. Hexasome-INO80 Complex Reveals Structural Basis of Noncanonical Nucleosome Remodeling. Science F6287 2023.
ISSN: ESSN 1095-9203
PubMed: 37384673
DOI: 10.1126/SCIENCE.ADF6287
Page generated: Thu Dec 28 10:02:35 2023

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