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Zinc in PDB 6re3: Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2B, Monomer-Masked Refinement

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

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

Other elements in 6re3:

The structure of Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2B, 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 2B, Monomer-Masked Refinement (pdb code 6re3). 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 2B, Monomer-Masked Refinement, PDB code: 6re3:

Zinc binding site 1 out of 1 in 6re3

Go back to Zinc Binding Sites List in 6re3
Zinc binding site 1 out of 1 in the Cryo-Em Structure of Polytomella F-Atp Synthase, Rotary Substate 2B, 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 2B, 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 3.1 42.5 1.0
CE1 M:HIS248 3.3 42.5 1.0
OD1 6:ASP102 3.6 41.7 1.0
NE2 M:HIS252 3.9 45.1 1.0
CD1 6:LEU105 4.1 39.5 1.0
CD2 M:HIS248 4.4 42.5 1.0
NE2 6:GLN93 4.5 34.4 1.0
CE1 M:HIS252 4.5 45.1 1.0
ND1 M:HIS248 4.6 42.5 1.0
CB M:GLU172 4.6 31.6 1.0
O M:ASN171 4.7 30.5 1.0
CG 6:ASP102 4.7 41.7 1.0
CD2 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 06:28:20 2024

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