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

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

Magnesium	(Mg)	1 atom
Fluorine	(F)	4 atoms

The binding sites of Aluminium 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 Aluminium atom.
In total only one binding site of Aluminium was determined in the Cryoem Structure INO80CORE Hexasome Complex Atpase-Dna Refinement STATE1, PDB code: 8oo9:

Aluminium 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 Aluminium with other atoms in the Al 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:Al2003 b:61.9 occ:1.00 AL G:ALF2003 0.0 61.9 1.0 O1B G:ADP2001 1.8 51.9 1.0 F2 G:ALF2003 1.8 70.9 1.0 F4 G:ALF2003 1.8 62.0 1.0 F3 G:ALF2003 1.8 62.5 1.0 F1 G:ALF2003 1.8 51.9 1.0 PB G:ADP2001 3.0 39.9 1.0 O2B G:ADP2001 3.4 58.6 1.0 MG G:MG2002 3.5 64.3 1.0 NH2 G:ARG1661 3.6 34.5 1.0 OE2 G:GLU1108 3.7 69.7 1.0 NH1 G:ARG1664 3.8 59.3 1.0 O3B G:ADP2001 4.0 52.6 1.0 O3A G:ADP2001 4.1 57.6 1.0 NH2 G:ARG1664 4.1 60.2 1.0 NZ G:LYS1003 4.3 48.6 1.0 N G:GLY1634 4.4 50.8 1.0 CA G:GLY1634 4.4 57.1 1.0 OE1 G:GLU1108 4.4 66.6 1.0 CZ G:ARG1664 4.4 57.9 1.0 CD G:GLU1108 4.4 71.3 1.0 OE1 G:GLN1657 4.5 61.6 1.0 CE G:LYS1003 4.7 45.6 1.0 CZ G:ARG1661 4.7 54.1 1.0 N G:GLY1000 4.7 44.2 1.0 O G:GLY1634 4.8 58.6 1.0 CA G:MET999 4.9 47.8 1.0 CG G:MET999 4.9 44.9 1.0

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