Magnesium in PDB 7w4n: Deactive State Ci From Q1-Nadh Dataset, Subclass 5

Enzymatic activity of Deactive State Ci From Q1-Nadh Dataset, Subclass 5

All present enzymatic activity of Deactive State Ci From Q1-Nadh Dataset, Subclass 5:
7.1.1.2;

Other elements in 7w4n:

The structure of Deactive State Ci From Q1-Nadh Dataset, Subclass 5 also contains other interesting chemical elements:

Iron (Fe) 28 atoms
Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Deactive State Ci From Q1-Nadh Dataset, Subclass 5 (pdb code 7w4n). 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 Deactive State Ci From Q1-Nadh Dataset, Subclass 5, PDB code: 7w4n:

Magnesium binding site 1 out of 1 in 7w4n

Go back to Magnesium Binding Sites List in 7w4n
Magnesium binding site 1 out of 1 in the Deactive State Ci From Q1-Nadh Dataset, Subclass 5


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Deactive State Ci From Q1-Nadh Dataset, Subclass 5 within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg804

b:1.6
occ:1.00
OE1 M:GLN133 2.5 29.4 1.0
O M:VAL228 2.7 32.1 1.0
O M:LEU231 2.8 29.9 1.0
O M:CYS226 3.0 31.1 1.0
O M:ILE223 3.0 34.3 1.0
CD M:GLN133 3.4 24.5 1.0
CB M:CYS226 3.7 17.3 1.0
C M:VAL228 3.8 19.7 1.0
NE2 M:GLN133 3.8 23.6 1.0
C M:CYS226 3.9 23.6 1.0
C M:LEU231 4.1 14.8 1.0
C M:ILE223 4.1 24.7 1.0
SG M:CYS226 4.2 21.0 1.0
CA M:CYS226 4.3 16.1 1.0
N M:VAL228 4.4 13.7 1.0
CA M:GLY229 4.4 11.0 1.0
N M:GLY229 4.6 7.8 1.0
CG2 M:ILE223 4.6 13.1 1.0
CA M:ILE223 4.7 20.0 1.0
N M:CYS226 4.7 21.8 1.0
C M:PRO227 4.7 13.8 1.0
CG M:GLN133 4.7 23.6 1.0
CA M:VAL228 4.7 24.4 1.0
N M:LEU231 4.7 20.6 1.0
CG2 M:THR232 4.8 19.6 1.0
CA M:LEU231 4.9 11.2 1.0
N M:PRO227 4.9 18.8 1.0
CE L:MET87 5.0 31.1 1.0

Reference:

J.Gu, T.Liu, R.Guo, L.Zhang, M.Yang. The Coupling Mechanism of Mammalian Mitochondrial Complex I Nat.Struct.Mol.Biol. V. 29 172 2022.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-022-00722-W
Page generated: Fri Apr 7 01:32:20 2023

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