Magnesium in PDB 8q45: Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng.

All present enzymatic activity of Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

The structure of Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng. also contains other interesting chemical elements:

Potassium	(K)	1 atom
Zinc	(Zn)	2 atoms
Iron	(Fe)	28 atoms

The binding sites of Magnesium atom in the Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng. (pdb code 8q45). 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 Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng., PDB code: 8q45:

Magnesium binding site 1 out of 1 in the Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Inward-Facing, Closed Proteoliposome Complex I at 2.7 A. Initially Purified in Lmng. within 5.0Å range: probe atom residue distance (Å) B Occ O:Mg402 b:55.3 occ:1.00 O1B O:DGT401 1.9 56.2 1.0 OG O:SER36 2.1 52.6 1.0 O1A O:DGT401 2.1 56.2 1.0 NZ O:LYS35 2.5 52.0 1.0 O1G O:DGT401 2.7 56.2 1.0 PB O:DGT401 3.0 56.2 1.0 PA O:DGT401 3.3 56.2 1.0 CB O:SER36 3.5 52.6 1.0 O3A O:DGT401 3.5 56.2 1.0 OE1 O:GLU125 3.5 49.8 1.0 OE1 O:GLU53 3.6 49.3 1.0 PG O:DGT401 3.8 56.2 1.0 CE O:LYS35 3.8 52.0 1.0 O3B O:DGT401 3.8 56.2 1.0 O2A O:DGT401 3.9 56.2 1.0 CA O:SER36 4.1 52.6 1.0 O2B O:DGT401 4.1 56.2 1.0 N O:SER36 4.1 52.6 1.0 CG O:LYS35 4.2 52.0 1.0 CD O:LYS35 4.4 52.0 1.0 O2G O:DGT401 4.5 56.2 1.0 O5' O:DGT401 4.5 56.2 1.0 CD O:GLU125 4.7 49.8 1.0 CD O:GLU53 4.7 49.3 1.0 O3G O:DGT401 4.9 56.2 1.0 CB O:GLU53 5.0 49.3 1.0

D.N.Grba, J.J.Wright, W.Fisher, Z.Yin, J.Hirst. Molecular Mechanism of the Ischemia-Induced Regulatory Switch in Mammalian Complex I Science 2024.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.ADO2075