Potassium in PDB 8q1y: Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng.

Enzymatic activity of Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng.

All present enzymatic activity of Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 8q1y:

The structure of Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng. also contains other interesting chemical elements:

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

Potassium Binding Sites:

The binding sites of Potassium atom in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng. (pdb code 8q1y). 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, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng., PDB code: 8q1y:

Potassium binding site 1 out of 1 in 8q1y

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Potassium Binding Sites List in 8q1y

Potassium binding site 1 out of 1 in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. 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 Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
G:K804 b:30.2 occ:1.00	O	G:VAL205	2.6	30.2	1.0
	OE1	G:GLN110	2.6	29.3	1.0
	O	G:LEU208	2.9	33.4	1.0
	O	G:CYS203	2.9	32.5	1.0
	O	G:ILE200	3.0	35.5	1.0
	CD	G:GLN110	3.5	29.3	1.0
	CB	G:CYS203	3.7	32.5	1.0
	C	G:VAL205	3.7	30.2	1.0
	C	G:CYS203	3.8	32.5	1.0
	NE2	G:GLN110	3.9	29.3	1.0
	C	G:LEU208	4.0	33.4	1.0
	SG	G:CYS203	4.1	32.5	1.0
	C	G:ILE200	4.1	35.5	1.0
	CA	G:CYS203	4.3	32.5	1.0
	N	G:VAL205	4.3	30.2	1.0
	CA	G:GLY206	4.5	30.2	1.0
	N	G:GLY206	4.5	30.2	1.0
	C	G:PRO204	4.5	30.6	1.0
	CA	G:VAL205	4.6	30.2	1.0
	CG2	G:THR209	4.6	33.7	1.0
	N	G:LEU208	4.6	33.4	1.0
	CG	G:GLN110	4.7	29.3	1.0
	CA	G:ILE200	4.7	35.5	1.0
	N	G:CYS203	4.7	32.5	1.0
	CG2	G:ILE200	4.7	35.5	1.0
	CA	G:LEU208	4.8	33.4	1.0
	O	G:PRO204	4.8	30.6	1.0
	CE	Q:MET45	4.8	30.4	1.0
	N	G:PRO204	4.9	30.6	1.0
	CB	G:LEU208	5.0	33.4	1.0
	N	G:THR209	5.0	33.7	1.0

Reference:

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

Page generated: Sat Aug 9 17:27:51 2025

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