Zinc in PDB 6rdc: Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map

Enzymatic activity of Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map

All present enzymatic activity of Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map:
7.1.2.2;

Other elements in 6rdc:

The structure of Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map (pdb code 6rdc). 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 Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map, PDB code: 6rdc:

Zinc binding site 1 out of 1 in 6rdc

Go back to Zinc Binding Sites List in 6rdc
Zinc binding site 1 out of 1 in the Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryoem Structure of Polytomella F-Atp Synthase, Primary Rotary State 2, Composite Map within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Zn600

b:99.9
occ:1.00
NE2 M:HIS248 2.1 56.7 1.0
NE2 M:HIS252 2.5 57.7 1.0
O 6:HOH203 3.0 49.8 1.0
CD2 M:HIS248 3.0 56.7 1.0
CE1 M:HIS248 3.1 56.7 1.0
CE1 M:HIS252 3.3 57.7 1.0
CD2 M:HIS252 3.6 57.7 1.0
OD1 6:ASP102 3.7 58.5 1.0
ND1 M:HIS248 4.2 56.7 1.0
CG M:HIS248 4.2 56.7 1.0
O 6:HOH204 4.2 60.1 1.0
CD1 6:LEU105 4.4 55.6 1.0
ND1 M:HIS252 4.5 57.7 1.0
CG M:HIS252 4.7 57.7 1.0
O M:HOH718 4.8 63.8 1.0
CG 6:ASP102 4.9 58.5 1.0
O M:HOH703 5.0 55.4 1.0
O M:HOH716 5.0 54.9 1.0
OE1 M:GLU172 5.0 48.7 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: Wed Dec 16 12:37:20 2020

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