Potassium in PDB 8q47: Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng.

All present enzymatic activity of Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

The structure of Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. 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 Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. (pdb code 8q47). 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, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng., PDB code: 8q47:

Potassium binding site 1 out of 1 in the Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Inward-Facing, OPEN1 Proteoliposome Complex I at 2.9 A. Initially Purified in Lmng. within 5.0Å range: probe atom residue distance (Å) B Occ G:K804 b:30.1 occ:1.00 O G:ILE200 2.6 34.1 1.0 O G:VAL205 2.8 29.8 1.0 OE1 G:GLN110 2.9 30.0 1.0 O G:LEU208 2.9 32.6 1.0 O G:CYS203 3.0 31.7 1.0 CE Q:MET45 3.4 32.5 1.0 CD G:GLN110 3.6 30.0 1.0 C G:ILE200 3.8 34.1 1.0 CB G:CYS203 3.8 31.7 1.0 NE2 G:GLN110 3.9 30.0 1.0 C G:CYS203 4.0 31.7 1.0 C G:VAL205 4.0 29.8 1.0 C G:LEU208 4.1 32.6 1.0 SG G:CYS203 4.4 31.7 1.0 CA G:CYS203 4.4 31.7 1.0 CG2 G:ILE200 4.4 34.1 1.0 CA G:ILE200 4.5 34.1 1.0 N G:VAL205 4.5 29.8 1.0 O G:ASP201 4.7 34.2 1.0 N G:CYS203 4.7 31.7 1.0 CA G:GLY206 4.8 30.5 1.0 CG2 G:THR209 4.8 32.7 1.0 N G:GLY206 4.8 30.5 1.0 CG G:GLN110 4.8 30.0 1.0 N G:ASP201 4.8 34.2 1.0 CA G:VAL205 4.9 29.8 1.0 C G:ASP201 4.9 34.2 1.0 CA G:ASP201 5.0 34.2 1.0 N G:LEU208 5.0 32.6 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