Magnesium in PDB 7vyh: Matrix Arm of Deactive State Ci From Rotenone Dataset

Enzymatic activity of Matrix Arm of Deactive State Ci From Rotenone Dataset

All present enzymatic activity of Matrix Arm of Deactive State Ci From Rotenone Dataset:
7.1.1.2;

Other elements in 7vyh:

The structure of Matrix Arm of Deactive State Ci From Rotenone Dataset 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 Matrix Arm of Deactive State Ci From Rotenone Dataset (pdb code 7vyh). 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 Matrix Arm of Deactive State Ci From Rotenone Dataset, PDB code: 7vyh:

Magnesium binding site 1 out of 1 in 7vyh

Go back to Magnesium Binding Sites List in 7vyh
Magnesium binding site 1 out of 1 in the Matrix Arm of Deactive State Ci 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 Matrix Arm of Deactive State Ci From Rotenone Dataset within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg804

b:6.7
occ:1.00
OE1 M:GLN133 2.6 11.2 1.0
O M:ILE223 2.8 15.0 1.0
O M:VAL228 2.9 12.5 1.0
O M:LEU231 2.9 12.2 1.0
O M:CYS226 3.0 13.0 1.0
CD M:GLN133 3.5 11.2 1.0
NE2 M:GLN133 3.8 11.2 1.0
CB M:CYS226 3.8 13.0 1.0
C M:VAL228 4.0 12.5 1.0
C M:ILE223 4.0 15.0 1.0
C M:CYS226 4.0 13.0 1.0
C M:LEU231 4.1 12.2 1.0
CE L:MET87 4.3 16.6 1.0
SG M:CYS226 4.4 13.0 1.0
CA M:CYS226 4.4 13.0 1.0
CG2 M:ILE223 4.5 15.0 1.0
CA M:ILE223 4.5 15.0 1.0
CA M:GLY229 4.5 10.6 1.0
N M:VAL228 4.7 12.5 1.0
CG2 M:THR232 4.7 14.4 1.0
N M:GLY229 4.7 10.6 1.0
N M:CYS226 4.8 13.0 1.0
CG M:GLN133 4.8 11.2 1.0
N M:LEU231 4.9 12.2 1.0
C M:PRO227 4.9 9.0 1.0
CA M:VAL228 5.0 12.5 1.0
CA M:LEU231 5.0 12.2 1.0

Reference:

J.K.Gu, T.Liu, R.Guo, L.Zhang, M.J.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 01:14:02 2023

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