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Magnesium in PDB 7v31: Active State Complex I From Rotenone Dataset

Enzymatic activity of Active State Complex I From Rotenone Dataset

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

Other elements in 7v31:

The structure of Active State Complex I From Rotenone 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 Rotenone Dataset (pdb code 7v31). 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 Rotenone Dataset, PDB code: 7v31:

Magnesium binding site 1 out of 1 in 7v31

Go back to Magnesium Binding Sites List in 7v31
Magnesium binding site 1 out of 1 in the Active State Complex I From Rotenone 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 Rotenone Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg804

b:25.7
occ:1.00
O M:ILE223 2.4 14.6 1.0
O M:LEU231 2.6 13.8 1.0
O M:CYS226 2.9 9.1 1.0
O M:VAL228 3.0 6.8 1.0
OE1 M:GLN133 3.1 13.5 1.0
CB M:CYS226 3.5 9.1 1.0
C M:ILE223 3.5 14.6 1.0
C M:LEU231 3.8 13.8 1.0
C M:CYS226 3.8 9.1 1.0
CD M:GLN133 3.9 13.5 1.0
SG M:CYS226 4.0 9.1 1.0
CA M:CYS226 4.1 9.1 1.0
CA M:ILE223 4.1 14.6 1.0
C M:VAL228 4.2 6.8 1.0
NE2 M:GLN133 4.2 13.5 1.0
CG2 M:ILE223 4.3 14.6 1.0
N M:CYS226 4.4 9.1 1.0
CA M:LEU231 4.6 13.8 1.0
N M:LEU231 4.6 13.8 1.0
N M:ASP224 4.7 15.2 1.0
CB M:LEU231 4.7 13.8 1.0
N M:VAL228 4.7 6.8 1.0
O M:ILE222 4.7 13.8 1.0
N M:THR232 4.7 14.1 1.0
CG2 M:THR232 4.8 14.1 1.0
CA M:THR232 4.8 14.1 1.0
CB M:ILE223 4.9 14.6 1.0
O M:ASP224 4.9 15.2 1.0
CA M:ASP224 4.9 15.2 1.0
N M:PRO227 4.9 6.3 1.0
CA M:GLY229 5.0 8.0 1.0
C M:ASP224 5.0 15.2 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: Thu Oct 3 10:21:02 2024

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