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Calcium in PDB 9ud6: Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State

Enzymatic activity of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State

All present enzymatic activity of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State:
7.2.1.1;

Other elements in 9ud6:

The structure of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State (pdb code 9ud6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State, PDB code: 9ud6:

Calcium binding site 1 out of 1 in 9ud6

Go back to Calcium Binding Sites List in 9ud6
Calcium binding site 1 out of 1 in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Upper State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca302

b:124.1
occ:1.00
NE2 C:GLN93 3.3 113.3 1.0
N C:ALA119 3.5 114.5 1.0
NE2 C:HIS141 3.8 88.9 1.0
CA C:ARG118 3.9 112.7 1.0
CB C:ALA97 4.0 121.0 1.0
CH2 C:TRP238 4.1 91.9 1.0
O C:ARG117 4.2 120.7 1.0
CB C:ALA119 4.2 116.2 1.0
C C:ARG118 4.2 117.0 1.0
CG C:GLN93 4.2 114.2 1.0
CD C:GLN93 4.3 116.2 1.0
CG C:ARG118 4.3 109.5 1.0
CZ2 C:TRP238 4.4 86.7 1.0
CA C:ALA119 4.5 115.1 1.0
CE1 C:HIS141 4.6 91.0 1.0
CB C:ARG118 4.7 110.8 1.0
O C:GLN93 4.8 120.4 1.0
CD2 C:HIS141 4.9 88.7 1.0
N C:ARG118 4.9 115.0 1.0
C C:ARG117 5.0 117.8 1.0

Reference:

M.Ishikawa-Fukuda, T.Seki, J.I.Kishikawa, M.Takahiro, K.I.Okazaki, T.Kato, B.Barquera, H.Miyoshi, M.Murai. The Na + -Pumping Mechanism Driven By Redox Reactions in the Nadh-Quinone Oxidoreductase From Vibrio Cholerae Relies on Dynamic Conformational Changes. Biorxiv 2025.
ISSN: ISSN 2692-8205
PubMed: 40501732
DOI: 10.1101/2025.06.01.656757
Page generated: Thu Jul 10 10:27:25 2025

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