Magnesium in PDB 7v2c: Active State Complex I From Q10 Dataset

Enzymatic activity of Active State Complex I From Q10 Dataset

All present enzymatic activity of Active State Complex I From Q10 Dataset:
7.1.1.2;

Other elements in 7v2c:

The structure of Active State Complex I From Q10 Dataset also contains other interesting chemical elements:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Active State Complex I From Q10 Dataset (pdb code 7v2c). 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 Active State Complex I From Q10 Dataset, PDB code: 7v2c:

Magnesium binding site 1 out of 1 in 7v2c

Go back to Magnesium Binding Sites List in 7v2c
Magnesium binding site 1 out of 1 in the Active State Complex I From Q10 Dataset


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Active State Complex I From Q10 Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg804

b:30.5
occ:1.00
O M:VAL228 2.7 34.9 1.0
O M:LEU231 2.7 37.9 1.0
OE1 M:GLN133 2.8 36.6 1.0
O M:ILE223 2.8 39.4 1.0
O M:CYS226 2.9 37.2 1.0
CD M:GLN133 3.7 36.6 1.0
CB M:CYS226 3.8 37.2 1.0
C M:CYS226 3.8 37.2 1.0
C M:VAL228 3.9 34.9 1.0
C M:LEU231 4.0 37.9 1.0
C M:ILE223 4.0 39.4 1.0
NE2 M:GLN133 4.1 36.6 1.0
SG M:CYS226 4.1 37.2 1.0
CA M:CYS226 4.3 37.2 1.0
N M:VAL228 4.4 34.9 1.0
CA M:ILE223 4.5 39.4 1.0
CG2 M:ILE223 4.5 39.4 1.0
N M:LEU231 4.7 37.9 1.0
N M:CYS226 4.7 37.2 1.0
CA M:GLY229 4.7 35.7 1.0
N M:GLY229 4.8 35.7 1.0
CA M:LEU231 4.8 37.9 1.0
CG2 M:THR232 4.8 39.1 1.0
CA M:VAL228 4.8 34.9 1.0
C M:PRO227 4.8 35.1 1.0
N M:PRO227 4.8 35.1 1.0
SD L:MET87 4.8 40.4 1.0
CB M:LEU231 4.9 37.9 1.0
CG M:GLN133 4.9 36.6 1.0
N M:THR232 4.9 39.1 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
PubMed: 35145322
DOI: 10.1038/S41594-022-00722-W
Page generated: Fri Apr 7 00:16:01 2023

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