Potassium in PDB 8q0m: Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.

All present enzymatic activity of Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

The structure of Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Zinc	(Zn)	2 atoms
Iron	(Fe)	28 atoms

The binding sites of Potassium atom in the Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. (pdb code 8q0m). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm., PDB code: 8q0m:

Potassium binding site 1 out of 1 in the Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Outward-Facing, Closed Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. within 5.0Å range: probe atom residue distance (Å) B Occ G:K804 b:31.4 occ:1.00 O G:LEU208 2.9 31.4 1.0 O G:ILE200 2.9 33.1 1.0 O G:VAL205 3.0 27.8 1.0 O G:CYS203 3.0 29.8 1.0 OE1 G:GLN110 3.1 27.1 1.0 CD G:GLN110 3.6 27.1 1.0 NE2 G:GLN110 3.7 27.1 1.0 C G:ILE200 4.0 33.1 1.0 CE Q:MET45 4.0 32.0 1.0 CB G:CYS203 4.1 29.8 1.0 C G:LEU208 4.1 31.4 1.0 C G:VAL205 4.1 27.8 1.0 C G:CYS203 4.1 29.8 1.0 CG2 G:ILE200 4.2 33.1 1.0 CG2 G:THR209 4.5 31.7 1.0 CA G:ILE200 4.5 33.1 1.0 SG G:CYS203 4.6 29.8 1.0 CA G:CYS203 4.6 29.8 1.0 CA G:GLY206 4.6 27.9 1.0 CG G:GLN110 4.7 27.1 1.0 N G:VAL205 4.8 27.8 1.0 N G:GLY206 4.8 27.9 1.0 N G:CYS203 4.9 29.8 1.0 N G:LEU208 4.9 31.4 1.0 CA G:THR209 4.9 31.7 1.0 N G:THR209 4.9 31.7 1.0 CA G:LEU208 5.0 31.4 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