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Magnesium in PDB 7v2k: Deactive State Complex I From Dq-Nadh Dataset

Enzymatic activity of Deactive State Complex I From Dq-Nadh Dataset

All present enzymatic activity of Deactive State Complex I From Dq-Nadh Dataset:
7.1.1.2;

Other elements in 7v2k:

The structure of Deactive State Complex I From Dq-Nadh 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 Deactive State Complex I From Dq-Nadh Dataset (pdb code 7v2k). 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 Complex I From Dq-Nadh Dataset, PDB code: 7v2k:

Magnesium binding site 1 out of 1 in 7v2k

Go back to Magnesium Binding Sites List in 7v2k
Magnesium binding site 1 out of 1 in the Deactive State Complex I From Dq-Nadh Dataset


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Deactive State Complex I From Dq-Nadh Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg805

b:23.2
occ:1.00
OE1 M:GLN133 2.4 8.6 1.0
O M:VAL228 2.4 23.2 1.0
O M:LEU231 2.8 23.2 1.0
O M:CYS226 2.9 4.0 1.0
O M:ILE223 3.1 7.1 1.0
CD M:GLN133 3.5 8.6 1.0
CB M:CYS226 3.6 4.0 1.0
C M:VAL228 3.6 23.2 1.0
C M:CYS226 3.8 4.0 1.0
NE2 M:GLN133 3.8 8.6 1.0
C M:LEU231 3.9 23.2 1.0
SG M:CYS226 4.0 4.0 1.0
C M:ILE223 4.2 7.1 1.0
CA M:CYS226 4.2 4.0 1.0
N M:VAL228 4.2 23.2 1.0
CA M:GLY229 4.4 20.1 1.0
N M:GLY229 4.5 20.1 1.0
CA M:VAL228 4.6 23.2 1.0
N M:LEU231 4.6 23.2 1.0
CG2 M:ILE223 4.6 7.1 1.0
CA M:ILE223 4.6 7.1 1.0
C M:PRO227 4.7 23.2 1.0
CG2 M:THR232 4.7 5.8 1.0
N M:CYS226 4.7 4.0 1.0
CA M:LEU231 4.7 23.2 1.0
CE L:MET87 4.8 10.1 1.0
N M:PRO227 4.8 23.2 1.0
CG M:GLN133 4.8 8.6 1.0
N M:THR232 4.9 5.8 1.0
CB M:LEU231 5.0 23.2 1.0
CA M:THR232 5.0 5.8 1.0
C M:GLY229 5.0 20.1 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: Thu Oct 3 10:21:00 2024

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