Zinc in PDB 7qsk: Bovine Complex I in Lipid Nanodisc, Active-Q10

Enzymatic activity of Bovine Complex I in Lipid Nanodisc, Active-Q10

All present enzymatic activity of Bovine Complex I in Lipid Nanodisc, Active-Q10:
1.6.5.3; 1.6.99.3; 7.1.1.2;

Other elements in 7qsk:

The structure of Bovine Complex I in Lipid Nanodisc, Active-Q10 also contains other interesting chemical elements:

Iron (Fe) 28 atoms
Potassium (K) 1 atom
Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Bovine Complex I in Lipid Nanodisc, Active-Q10 (pdb code 7qsk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Bovine Complex I in Lipid Nanodisc, Active-Q10, PDB code: 7qsk:

Zinc binding site 1 out of 1 in 7qsk

Go back to Zinc Binding Sites List in 7qsk
Zinc binding site 1 out of 1 in the Bovine Complex I in Lipid Nanodisc, Active-Q10


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bovine Complex I in Lipid Nanodisc, Active-Q10 within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Zn201

b:53.1
occ:1.00
NE2 R:HIS68 2.0 34.5 1.0
SG R:CYS87 2.2 36.8 1.0
SG R:CYS84 2.2 38.4 1.0
SG R:CYS59 2.3 37.9 1.0
CE1 R:HIS68 2.8 34.5 1.0
CD2 R:HIS68 3.1 34.5 1.0
CB R:CYS84 3.2 38.4 1.0
CB R:CYS87 3.3 36.8 1.0
CB R:CYS59 3.3 37.9 1.0
N R:CYS87 3.8 36.8 1.0
N R:GLY61 3.9 38.3 1.0
ND1 R:HIS68 4.0 34.5 1.0
CA R:GLY61 4.1 38.3 1.0
CG R:HIS68 4.1 34.5 1.0
CA R:CYS87 4.2 36.8 1.0
C R:CYS59 4.3 37.9 1.0
CA R:CYS59 4.4 37.9 1.0
O R:CYS59 4.4 37.9 1.0
CB R:TYR86 4.6 33.7 1.0
C R:ASP60 4.6 38.8 1.0
CA R:CYS84 4.7 38.4 1.0
N R:ASP60 4.7 38.8 1.0
C R:TYR86 4.9 33.7 1.0
C R:CYS87 5.0 36.8 1.0

Reference:

I.Chung, J.J.Wright, H.R.Bridges, B.S.Ivanov, O.Biner, C.S.Pereira, G.M.Arantes, J.Hirst. Cryo-Em Structures Define Ubiquinone-10 Binding to Mitochondrial Complex I and Conformational Transitions Accompanying Q-Site Occupancy. Nat Commun V. 13 2758 2022.
ISSN: ESSN 2041-1723
PubMed: 35589726
DOI: 10.1038/S41467-022-30506-1
Page generated: Wed Oct 30 10:01:10 2024

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