Magnesium in PDB 8q4a: Outward-Facing, OPEN1 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.

Enzymatic activity of Outward-Facing, OPEN1 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.

All present enzymatic activity of Outward-Facing, OPEN1 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 8q4a:

The structure of Outward-Facing, OPEN1 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Outward-Facing, OPEN1 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. (pdb code 8q4a). 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 2.6 A. Initially Purified in Lmng., PDB code: 8q4a:

Magnesium binding site 1 out of 1 in 8q4a

Go back to Magnesium Binding Sites List in 8q4a
Magnesium binding site 1 out of 1 in the Outward-Facing, OPEN1 Proteoliposome Complex I at 2.6 A. 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 2.6 A. Initially Purified in Lmng. within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Mg402

b:69.2
occ:1.00
O1G O:DGT401 2.0 68.9 1.0
O1B O:DGT401 2.1 68.9 1.0
O1A O:DGT401 2.1 68.9 1.0
OG O:SER36 2.7 67.2 1.0
PB O:DGT401 3.1 68.9 1.0
PG O:DGT401 3.1 68.9 1.0
PA O:DGT401 3.2 68.9 1.0
O3B O:DGT401 3.6 68.9 1.0
O3A O:DGT401 3.6 68.9 1.0
O5' O:DGT401 3.7 68.9 1.0
O3G O:DGT401 3.7 68.9 1.0
OE1 O:GLU53 3.8 63.0 1.0
CB O:SER36 4.0 67.2 1.0
C5' O:DGT401 4.1 68.9 1.0
O2G O:DGT401 4.2 68.9 1.0
O2B O:DGT401 4.3 68.9 1.0
O2A O:DGT401 4.3 68.9 1.0
OE1 O:GLU125 4.7 63.9 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: Fri Oct 4 16:33:55 2024

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