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Zinc in PDB 7vbz: Matrix Arm of Active State Ci From Rotenone-Nadh Dataset

Enzymatic activity of Matrix Arm of Active State Ci From Rotenone-Nadh Dataset

All present enzymatic activity of Matrix Arm of Active State Ci From Rotenone-Nadh Dataset:
7.1.1.2;

Other elements in 7vbz:

The structure of Matrix Arm of Active State Ci From Rotenone-Nadh Dataset also contains other interesting chemical elements:

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

Zinc Binding Sites:

The binding sites of Zinc atom in the Matrix Arm of Active State Ci From Rotenone-Nadh Dataset (pdb code 7vbz). 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 Matrix Arm of Active State Ci From Rotenone-Nadh Dataset, PDB code: 7vbz:

Zinc binding site 1 out of 1 in 7vbz

Go back to Zinc Binding Sites List in 7vbz
Zinc binding site 1 out of 1 in the Matrix Arm of Active State Ci From Rotenone-Nadh Dataset


Mono view


Stereo pair view

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

b:27.8
occ:1.00
NE2 T:HIS95 2.3 11.3 1.0
SG T:CYS86 2.3 14.2 1.0
SG T:CYS111 2.3 15.0 1.0
CB T:CYS114 2.7 17.6 1.0
CB T:CYS111 3.2 15.0 1.0
CE1 T:HIS95 3.2 11.3 1.0
CD2 T:HIS95 3.2 11.3 1.0
CB T:CYS86 3.5 14.2 1.0
N T:CYS114 3.6 17.6 1.0
CA T:CYS114 3.7 17.6 1.0
N T:GLY88 3.9 14.4 1.0
SG T:CYS114 4.0 17.6 1.0
CA T:GLY88 4.1 14.4 1.0
ND1 T:HIS95 4.3 11.3 1.0
CG T:HIS95 4.4 11.3 1.0
CB T:TYR113 4.5 11.4 1.0
C T:CYS86 4.5 14.2 1.0
CA T:CYS86 4.6 14.2 1.0
N T:ASP87 4.6 14.4 1.0
C T:TYR113 4.6 11.4 1.0
C T:CYS114 4.6 17.6 1.0
CA T:CYS111 4.7 15.0 1.0
C T:ASP87 4.7 14.4 1.0
N T:GLY115 4.8 16.2 1.0
CD1 T:LEU116 4.8 16.9 1.0
O T:CYS86 4.9 14.2 1.0
CA T:TYR113 5.0 11.4 1.0
N T:TYR113 5.0 11.4 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 12:37:59 2024

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