Magnesium in PDB 8q25: Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng.

Enzymatic activity of Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng.

All present enzymatic activity of Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 8q25:

The structure of Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng. also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng. (pdb code 8q25). 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 Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng., PDB code: 8q25:

Magnesium binding site 1 out of 1 in 8q25

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Magnesium Binding Sites List in 8q25

Magnesium binding site 1 out of 1 in the Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. 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 Outward-Facing, OPEN1 Proteoliposome Complex I at 2.8 A, After Deactivation Treatment. Initially Purified in Lmng. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
O:Mg401 b:89.8 occ:1.00	O1B	O:DGT402	2.0	88.8	1.0
	O1G	O:DGT402	2.1	88.8	1.0
	O1A	O:DGT402	2.3	88.8	1.0
	PB	O:DGT402	3.1	88.8	1.0
	PG	O:DGT402	3.2	88.8	1.0
	PA	O:DGT402	3.4	88.8	1.0
	O3B	O:DGT402	3.5	88.8	1.0
	OG	O:SER36	3.6	89.9	1.0
	O3A	O:DGT402	3.7	88.8	1.0
	O3G	O:DGT402	3.8	88.8	1.0
	O5'	O:DGT402	4.1	88.8	1.0
	C5'	O:DGT402	4.1	88.8	1.0
	O2B	O:DGT402	4.2	88.8	1.0
	O2G	O:DGT402	4.4	88.8	1.0
	O2A	O:DGT402	4.5	88.8	1.0
	CB	O:SER36	4.8	89.9	1.0
	OE1	O:GLU53	4.9	80.0	1.0

Reference:

D.N.Grba, J.J.Wright, W.Fisher, Z.Yin, J.Hirst. Structure of Complex I Embedded in Liposomes Reveals Mechanism of Active/Deactive Transition Science 2024.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.ADO2075

Page generated: Fri Oct 4 16:30:05 2024

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