Zinc in PDB 7w1u: Active State Ci From Rotenone Dataset, Subclass 2

Enzymatic activity of Active State Ci From Rotenone Dataset, Subclass 2

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

Other elements in 7w1u:

The structure of Active State Ci From Rotenone 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 Active State Ci From Rotenone Dataset, Subclass 2 (pdb code 7w1u). 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 Active State Ci From Rotenone Dataset, Subclass 2, PDB code: 7w1u:

Zinc binding site 1 out of 1 in 7w1u

Go back to Zinc Binding Sites List in 7w1u
Zinc binding site 1 out of 1 in the Active State Ci From Rotenone 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 Active State Ci From Rotenone Dataset, Subclass 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
T:Zn201

b:42.7
occ:1.00
SG T:CYS86 2.3 23.1 1.0
SG T:CYS111 2.3 25.7 1.0
NE2 T:HIS95 2.3 17.2 1.0
CB T:CYS114 2.7 27.1 1.0
CE1 T:HIS95 3.1 17.2 1.0
CB T:CYS111 3.2 25.7 1.0
CD2 T:HIS95 3.4 17.2 1.0
CB T:CYS86 3.5 23.1 1.0
N T:CYS114 3.5 27.1 1.0
CA T:CYS114 3.7 27.1 1.0
N T:GLY88 3.9 20.1 1.0
SG T:CYS114 4.0 27.1 1.0
CA T:GLY88 4.1 20.1 1.0
ND1 T:HIS95 4.3 17.2 1.0
CG T:HIS95 4.4 17.2 1.0
C T:CYS86 4.6 23.1 1.0
CB T:TYR113 4.6 15.9 1.0
C T:CYS114 4.6 27.1 1.0
CA T:CYS86 4.6 23.1 1.0
CA T:CYS111 4.6 25.7 1.0
C T:TYR113 4.6 15.9 1.0
O T:CYS86 4.8 23.1 1.0
C T:ASP87 4.8 21.5 1.0
N T:GLY115 4.8 28.5 1.0
N T:ASP87 4.8 21.5 1.0
CB T:LEU116 4.9 31.2 1.0
N T:TYR113 5.0 15.9 1.0
CD1 T:LEU116 5.0 31.2 1.0
CA T:TYR113 5.0 15.9 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: Sat Apr 8 05:05:39 2023

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