Zinc in PDB 7w2l: Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2

Enzymatic activity of Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2

All present enzymatic activity of Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2:
7.1.1.2;

Other elements in 7w2l:

The structure of Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2 also contains other interesting chemical elements:

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

Zinc Binding Sites:

The binding sites of Zinc atom in the Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2 (pdb code 7w2l). 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 Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2, PDB code: 7w2l:

Zinc binding site 1 out of 1 in 7w2l

Go back to Zinc Binding Sites List in 7w2l
Zinc binding site 1 out of 1 in the Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Deactive State Ci From Rotenone-Nadh Dataset, Subclass 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
T:Zn201

b:43.2
occ:1.00
SG T:CYS111 2.3 16.8 1.0
NE2 T:HIS95 2.3 21.8 1.0
SG T:CYS86 2.3 13.8 1.0
CB T:CYS114 2.6 18.9 1.0
CB T:CYS111 3.1 11.9 1.0
CE1 T:HIS95 3.1 16.6 1.0
CD2 T:HIS95 3.4 21.9 1.0
N T:CYS114 3.5 28.4 1.0
CA T:CYS114 3.6 20.2 1.0
CB T:CYS86 3.7 9.4 1.0
N T:GLY88 3.9 15.0 1.0
SG T:CYS114 3.9 50.7 1.0
CA T:GLY88 3.9 8.5 1.0
ND1 T:HIS95 4.3 18.0 1.0
CG T:HIS95 4.4 16.2 1.0
C T:CYS114 4.5 17.1 1.0
CA T:CYS111 4.6 11.5 1.0
C T:CYS86 4.7 17.4 1.0
N T:GLY115 4.7 9.5 1.0
C T:TYR113 4.7 10.1 1.0
C T:ASP87 4.8 17.1 1.0
CA T:CYS86 4.8 8.3 1.0
CB T:TYR113 4.8 9.4 1.0
O T:CYS86 4.9 23.6 1.0
CB T:LEU116 4.9 11.7 1.0
N T:ASP87 4.9 18.8 1.0
N T:LEU116 5.0 13.0 1.0
CD1 T:LEU116 5.0 10.5 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: Wed Oct 30 13:35:46 2024

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