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Magnesium in PDB 8q49: Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng.

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

All present enzymatic activity of Outward-Facing, OPEN2 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 8q49:

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

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Outward-Facing, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng. (pdb code 8q49). 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, OPEN2 Proteoliposome Complex I at 2.6 A. Initially Purified in Lmng., PDB code: 8q49:

Magnesium binding site 1 out of 1 in 8q49

Go back to Magnesium Binding Sites List in 8q49
Magnesium binding site 1 out of 1 in the Outward-Facing, OPEN2 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, OPEN2 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:58.2
occ:1.00
O1A O:DGT401 2.3 58.9 1.0
O1G O:DGT401 2.6 58.9 1.0
O1B O:DGT401 2.8 58.9 1.0
OG O:SER36 2.9 57.0 1.0
PA O:DGT401 3.5 58.9 1.0
PB O:DGT401 3.6 58.9 1.0
PG O:DGT401 3.7 58.9 1.0
O3A O:DGT401 3.8 58.9 1.0
O3B O:DGT401 3.8 58.9 1.0
OE1 O:GLU53 3.9 51.8 1.0
C5' O:DGT401 4.2 58.9 1.0
CB O:SER36 4.3 57.0 1.0
O3G O:DGT401 4.3 58.9 1.0
O5' O:DGT401 4.4 58.9 1.0
O2A O:DGT401 4.5 58.9 1.0
O2G O:DGT401 4.8 58.9 1.0
OE1 O:GLU125 4.8 53.2 1.0
O2B O:DGT401 4.9 58.9 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 16:33:48 2024

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