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Zinc in PDB 6re9: Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement

Enzymatic activity of Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement

All present enzymatic activity of Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement:
7.1.2.2;

Other elements in 6re9:

The structure of Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement (pdb code 6re9). 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 Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement, PDB code: 6re9:

Zinc binding site 1 out of 1 in 6re9

Go back to Zinc Binding Sites List in 6re9
Zinc binding site 1 out of 1 in the Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2D, Monomer-Masked Refinement within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Zn600

b:50.0
occ:1.00
 NE2 M:HIS248 2.4 42.5 1.0
NE2 M:HIS252 2.7 45.1 1.0
CE1 M:HIS248 2.8 42.5 1.0
CE1 M:HIS252 3.5 45.1 1.0
CD2 M:HIS248 3.7 42.5 1.0
CD2 M:HIS252 3.9 45.1 1.0
ND1 M:HIS248 4.0 42.5 1.0
OD1 6:ASP102 4.2 41.7 1.0
CD1 6:LEU105 4.4 39.5 1.0
CG M:HIS248 4.5 42.5 1.0
CG 6:ASP102 4.6 41.7 1.0
ND1 M:HIS252 4.7 45.1 1.0
OD2 6:ASP102 4.9 41.7 1.0
CG M:HIS252 4.9 45.1 1.0

Reference:

B.J.Murphy, N.Klusch, J.Langer, D.J.Mills, O.Yildiz, W.Kuhlbrandt. Rotary Substates of Mitochondrial Atp Synthase Reveal the Basis of Flexible F1-Focoupling. Science V. 364 2019.
ISSN: ESSN 1095-9203
PubMed: 31221832
DOI: 10.1126/SCIENCE.AAW9128
Page generated: Tue Oct 29 06:29:12 2024

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