Potassium in PDB 8q0f: Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm.

All present enzymatic activity of Inward-Facing, OPEN2 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 Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. also contains other interesting chemical elements:

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

The binding sites of Potassium atom in the Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm. (pdb code 8q0f). 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 Inward-Facing, OPEN2 Proteoliposome Complex I at 3.1 A. Initially Purified in Ddm., PDB code: 8q0f:

Potassium binding site 1 out of 1 in the Inward-Facing, OPEN2 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 Inward-Facing, OPEN2 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:29.0 occ:1.00 OE1 G:GLN110 2.6 21.9 1.0 O G:VAL205 2.7 23.6 1.0 O G:CYS203 2.8 26.1 1.0 O G:ILE200 2.9 30.5 1.0 O G:LEU208 3.0 28.2 1.0 CD G:GLN110 3.3 21.9 1.0 NE2 G:GLN110 3.6 21.9 1.0 C G:CYS203 3.7 26.1 1.0 CB G:CYS203 3.8 26.1 1.0 C G:VAL205 3.8 23.6 1.0 C G:ILE200 4.1 30.5 1.0 C G:LEU208 4.2 28.2 1.0 SG G:CYS203 4.2 26.1 1.0 N G:VAL205 4.3 23.6 1.0 CA G:CYS203 4.3 26.1 1.0 CE Q:MET45 4.4 26.1 1.0 CG2 G:THR209 4.5 27.3 1.0 CG G:GLN110 4.5 21.9 1.0 C G:PRO204 4.6 24.5 1.0 CA G:VAL205 4.7 23.6 1.0 N G:CYS203 4.7 26.1 1.0 N G:GLY206 4.7 23.6 1.0 N G:PRO204 4.7 24.5 1.0 CA G:ILE200 4.7 30.5 1.0 O G:ASP201 4.8 30.6 1.0 CA G:GLY206 4.8 23.6 1.0 CG2 G:ILE200 4.8 30.5 1.0 N G:LEU208 4.9 28.2 1.0 CA G:PRO204 5.0 24.5 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