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Iron in PDB 9ud8: Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State

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

Other elements in 9ud8:

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

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State (pdb code 9ud8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State, PDB code: 9ud8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 9ud8

Go back to Iron Binding Sites List in 9ud8
Iron binding site 1 out of 4 in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe 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+, Middle State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:63.5
occ:1.00
FE1 E:FES301 0.0 63.5 1.0
S1 E:FES301 2.2 63.5 1.0
S2 E:FES301 2.2 63.5 1.0
SG D:CYS112 2.3 34.3 1.0
FE2 E:FES301 2.7 63.5 1.0
SG E:CYS26 3.2 25.8 1.0
SG E:CYS120 3.2 21.3 1.0
CB D:CYS112 3.2 34.3 1.0
CB E:CYS26 3.7 25.8 1.0
N D:CYS112 3.9 34.3 1.0
CA D:CYS112 4.1 34.3 1.0
N D:GLY27 4.5 30.9 1.0
CB E:CYS120 4.7 21.3 1.0
O D:THR110 4.7 27.7 1.0
SG D:CYS29 4.8 21.1 1.0
N E:CYS26 4.9 25.8 1.0
CA E:CYS26 4.9 25.8 1.0
CA D:GLY27 4.9 30.9 1.0
C D:ASN111 5.0 17.2 1.0
CD1 D:LEU26 5.0 39.7 1.0

Iron binding site 2 out of 4 in 9ud8

Go back to Iron Binding Sites List in 9ud8
Iron binding site 2 out of 4 in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe301

b:63.5
occ:1.00
FE2 E:FES301 0.0 63.5 1.0
S2 E:FES301 2.2 63.5 1.0
S1 E:FES301 2.2 63.5 1.0
SG D:CYS29 2.3 21.1 1.0
SG E:CYS120 2.3 21.3 1.0
CB D:CYS29 2.7 21.1 1.0
FE1 E:FES301 2.7 63.5 1.0
CB E:CYS120 3.4 21.3 1.0
N D:CYS29 3.6 21.1 1.0
CA D:CYS29 3.7 21.1 1.0
N E:GLY24 4.4 10.5 1.0
N D:VAL28 4.6 27.7 1.0
CA E:GLY24 4.7 10.5 1.0
C D:VAL28 4.8 27.7 1.0
N E:MET25 4.8 29.6 1.0
CA E:CYS120 4.8 21.3 1.0
C D:CYS29 4.9 21.1 1.0
SG D:CYS112 5.0 34.3 1.0
N E:CYS26 5.0 25.8 1.0

Iron binding site 3 out of 4 in 9ud8

Go back to Iron Binding Sites List in 9ud8
Iron binding site 3 out of 4 in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:156.5
occ:1.00
FE1 F:FES501 0.0 156.5 1.0
S2 F:FES501 2.2 156.5 1.0
S1 F:FES501 2.2 156.5 1.0
SG F:CYS79 2.3 110.2 1.0
SG F:CYS111 2.3 113.0 1.0
FE2 F:FES501 2.7 156.5 1.0
CB F:CYS79 3.3 110.2 1.0
CB F:CYS111 3.5 113.0 1.0
N F:GLY72 3.8 94.0 1.0
CA F:GLY72 3.9 94.0 1.0
C F:GLY71 4.3 90.8 1.0
SG F:CYS70 4.4 108.6 1.0
N F:CYS79 4.5 110.2 1.0
CA F:CYS79 4.5 110.2 1.0
N F:CYS111 4.5 113.0 1.0
C F:GLY72 4.6 94.0 1.0
SG F:CYS76 4.6 115.4 1.0
CA F:CYS111 4.6 113.0 1.0
O F:GLY71 4.7 90.8 1.0
CD2 F:LEU56 4.8 93.3 1.0
N F:GLY71 4.8 90.8 1.0
CA F:GLY71 4.8 90.8 1.0
OE1 F:GLN112 4.9 114.2 1.0
O F:GLY72 4.9 94.0 1.0
N F:GLY77 5.0 112.0 1.0

Iron binding site 4 out of 4 in 9ud8

Go back to Iron Binding Sites List in 9ud8
Iron binding site 4 out of 4 in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, in the Absence of Na+, Middle State within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:156.5
occ:1.00
FE2 F:FES501 0.0 156.5 1.0
S2 F:FES501 2.2 156.5 1.0
S1 F:FES501 2.2 156.5 1.0
SG F:CYS76 2.3 115.4 1.0
SG F:CYS70 2.3 108.6 1.0
FE1 F:FES501 2.7 156.5 1.0
CB F:CYS76 3.7 115.4 1.0
N F:GLY77 3.7 112.0 1.0
N F:CYS76 3.8 115.4 1.0
CB F:CYS70 4.0 108.6 1.0
CA F:CYS76 4.2 115.4 1.0
N F:GLY71 4.2 90.8 1.0
SG F:CYS79 4.2 110.2 1.0
N F:GLY72 4.2 94.0 1.0
N F:CYS70 4.2 108.6 1.0
C F:CYS76 4.4 115.4 1.0
N F:GLN78 4.5 116.2 1.0
O F:GLY72 4.5 94.0 1.0
CA F:CYS70 4.5 108.6 1.0
CA F:GLY77 4.6 112.0 1.0
OG F:SER68 4.7 104.3 1.0
N F:SER75 4.7 107.7 1.0
C F:CYS70 4.7 108.6 1.0
N F:ALA69 4.7 106.7 1.0
CA F:GLY72 4.7 94.0 1.0
C F:GLY72 4.9 94.0 1.0
SG F:CYS111 4.9 113.0 1.0
N F:CYS79 4.9 110.2 1.0
CB F:CYS79 4.9 110.2 1.0
C F:GLY71 4.9 90.8 1.0
CA F:GLY71 5.0 90.8 1.0
C F:GLY77 5.0 112.0 1.0
C F:SER75 5.0 107.7 1.0

Reference:

M.Ishikawa-Fukuda, T.Seki, J.I.Kishikawa, T.Masuya, 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: Sat Aug 23 03:29:26 2025

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