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Iron in PDB 28pn: Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.

Enzymatic activity of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.

All present enzymatic activity of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.:
1.7.2.5;

Other elements in 28pn:

The structure of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. (pdb code 28pn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 6 binding sites of Iron where determined in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid., PDB code: 28pn:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6;

Iron binding site 1 out of 6 in 28pn

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Iron binding site 1 out of 6 in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:43.0
occ:1.00
 FE A:HEM801 0.0 43.0 1.0
NE2 A:HIS331 2.0 28.0 1.0
NB A:HEM801 2.1 29.0 1.0
NC A:HEM801 2.1 27.7 1.0
ND A:HEM801 2.1 26.9 1.0
NA A:HEM801 2.1 29.6 1.0
NE2 A:HIS631 2.6 23.1 1.0
CE1 A:HIS331 2.9 26.7 1.0
CD2 A:HIS331 3.0 23.9 1.0
C1D A:HEM801 3.1 25.4 1.0
C4C A:HEM801 3.1 24.1 1.0
C1B A:HEM801 3.1 29.1 1.0
C4A A:HEM801 3.1 24.9 1.0
C1A A:HEM801 3.1 26.2 1.0
C4D A:HEM801 3.1 24.5 1.0
C1C A:HEM801 3.1 26.0 1.0
C4B A:HEM801 3.1 28.0 1.0
CD2 A:HIS631 3.4 23.3 1.0
CHD A:HEM801 3.4 22.2 1.0
CHB A:HEM801 3.4 26.6 1.0
CHA A:HEM801 3.5 21.3 1.0
CHC A:HEM801 3.5 26.5 1.0
CE1 A:HIS631 3.6 27.5 1.0
ND1 A:HIS331 4.0 31.2 1.0
CG A:HIS331 4.1 27.5 1.0
C2D A:HEM801 4.3 26.9 1.0
C3D A:HEM801 4.3 26.1 1.0
C3C A:HEM801 4.3 26.2 1.0
C3A A:HEM801 4.3 23.2 1.0
C2B A:HEM801 4.3 30.2 1.0
C2A A:HEM801 4.3 24.9 1.0
C2C A:HEM801 4.3 24.5 1.0
C3B A:HEM801 4.3 28.2 1.0
CG A:HIS631 4.5 24.4 1.0
ND1 A:HIS631 4.6 29.3 1.0
NE2 A:GLN296 4.9 28.5 1.0

Iron binding site 2 out of 6 in 28pn

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Iron binding site 2 out of 6 in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe803

b:52.4
occ:1.00
 FE A:HEM803 0.0 52.4 1.0
NA A:HEM803 2.0 37.3 1.0
NC A:HEM803 2.1 41.9 1.0
ND A:HEM803 2.1 37.9 1.0
NB A:HEM803 2.1 38.8 1.0
O A:HOH1011 2.1 36.9 1.0
NE2 A:HIS629 2.6 31.4 1.0
C4D A:HEM803 3.0 35.5 1.0
C1A A:HEM803 3.1 29.0 1.0
C1D A:HEM803 3.1 33.8 1.0
C4B A:HEM803 3.1 39.0 1.0
C1C A:HEM803 3.1 43.8 1.0
C4A A:HEM803 3.1 34.2 1.0
C4C A:HEM803 3.1 41.7 1.0
C1B A:HEM803 3.1 33.9 1.0
CD2 A:HIS629 3.3 28.3 1.0
CHA A:HEM803 3.4 30.3 1.0
CHC A:HEM803 3.4 42.4 1.0
CHD A:HEM803 3.4 37.9 1.0
CHB A:HEM803 3.5 34.3 1.0
FE A:FE804 3.5 84.1 1.0
CE1 A:HIS629 3.8 33.7 1.0
C3D A:HEM803 4.2 35.2 1.0
C2D A:HEM803 4.3 34.9 1.0
C2A A:HEM803 4.3 28.1 1.0
C3A A:HEM803 4.3 31.0 1.0
C3B A:HEM803 4.3 37.9 1.0
C2C A:HEM803 4.3 43.8 1.0
C2B A:HEM803 4.3 33.0 1.0
C3C A:HEM803 4.3 44.8 1.0
CG A:HIS629 4.5 31.9 1.0
CE1 A:HIS537 4.7 44.6 1.0
ND1 A:HIS629 4.7 37.1 1.0

Iron binding site 3 out of 6 in 28pn

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Iron binding site 3 out of 6 in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe804

b:84.1
occ:1.00
 O A:HOH1011 1.9 36.9 1.0
NE2 A:HIS486 2.3 70.9 1.0
NE2 A:HIS537 2.4 45.3 1.0
CE1 A:HIS537 2.5 44.6 1.0
CE1 A:HIS486 2.9 68.5 1.0
NE2 A:HIS538 3.1 34.2 1.0
FE A:HEM803 3.5 52.4 1.0
CD2 A:HIS486 3.6 58.7 1.0
CD2 A:HIS537 3.8 48.5 1.0
ND1 A:HIS537 3.8 44.1 1.0
NC A:HEM803 3.8 41.9 1.0
CE1 A:HIS538 3.9 31.5 1.0
CD2 A:HIS538 3.9 34.6 1.0
ND A:HEM803 4.0 37.9 1.0
O A:GLY534 4.1 56.1 1.0
C1D A:HEM803 4.1 33.8 1.0
C4C A:HEM803 4.1 41.7 1.0
ND1 A:HIS486 4.1 67.3 1.0
CHD A:HEM803 4.3 37.9 1.0
CG A:HIS537 4.4 41.1 1.0
C1C A:HEM803 4.4 43.8 1.0
CG A:HIS486 4.5 62.0 1.0
C4D A:HEM803 4.5 35.5 1.0
OE1 A:GLU490 4.6 69.2 1.0
NB A:HEM803 4.6 38.8 1.0
NA A:HEM803 4.7 37.3 1.0
CA A:GLY534 4.7 56.3 1.0
C A:GLY534 4.8 55.7 1.0
C2D A:HEM803 4.8 34.9 1.0
CHC A:HEM803 4.9 42.4 1.0
ND1 A:HIS538 5.0 35.6 1.0
C3C A:HEM803 5.0 44.8 1.0

Iron binding site 4 out of 6 in 28pn

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Iron binding site 4 out of 6 in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:54.6
occ:1.00
 FE B:HEM801 0.0 54.6 1.0
NA B:HEM801 2.1 39.6 1.0
NC B:HEM801 2.1 48.4 1.0
NB B:HEM801 2.1 41.6 1.0
ND B:HEM801 2.1 39.3 1.0
O B:HOH1000 2.1 42.9 1.0
NE2 B:HIS629 2.6 31.9 1.0
C4D B:HEM801 3.0 38.3 1.0
C1D B:HEM801 3.1 36.6 1.0
C1A B:HEM801 3.1 31.4 1.0
C4B B:HEM801 3.1 43.5 1.0
C1C B:HEM801 3.1 49.4 1.0
C4A B:HEM801 3.1 34.5 1.0
C4C B:HEM801 3.1 46.5 1.0
C1B B:HEM801 3.1 37.0 1.0
CD2 B:HIS629 3.3 30.9 1.0
CHA B:HEM801 3.4 32.9 1.0
CHC B:HEM801 3.4 48.5 1.0
FE B:FE803 3.4 87.2 1.0
CHD B:HEM801 3.4 41.4 1.0
CHB B:HEM801 3.5 35.1 1.0
CE1 B:HIS629 3.7 33.8 1.0
C3D B:HEM801 4.2 38.0 1.0
C2D B:HEM801 4.2 39.0 1.0
C2A B:HEM801 4.3 29.4 1.0
C3A B:HEM801 4.3 31.0 1.0
C3B B:HEM801 4.3 41.7 1.0
C2C B:HEM801 4.3 49.1 1.0
C2B B:HEM801 4.3 35.7 1.0
C3C B:HEM801 4.3 46.5 1.0
CG B:HIS629 4.6 34.1 1.0
ND1 B:HIS629 4.7 37.9 1.0

Iron binding site 5 out of 6 in 28pn

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Iron binding site 5 out of 6 in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe803

b:87.2
occ:1.00
 O B:HOH1000 1.9 42.9 1.0
NE2 B:HIS486 2.3 65.9 1.0
NE2 B:HIS537 2.4 44.3 1.0
CE1 B:HIS486 2.9 63.8 1.0
CE1 B:HIS537 2.9 46.7 1.0
NE2 B:HIS538 3.1 33.6 1.0
FE B:HEM801 3.4 54.6 1.0
CD2 B:HIS486 3.5 54.5 1.0
CD2 B:HIS537 3.7 46.5 1.0
NC B:HEM801 3.7 48.4 1.0
CE1 B:HIS538 3.9 31.8 1.0
ND B:HEM801 4.0 39.3 1.0
O B:GLY534 4.0 56.9 1.0
CD2 B:HIS538 4.0 33.8 1.0
ND1 B:HIS486 4.1 58.4 1.0
C1D B:HEM801 4.1 36.6 1.0
C4C B:HEM801 4.1 46.5 1.0
ND1 B:HIS537 4.2 46.8 1.0
CHD B:HEM801 4.3 41.4 1.0
C1C B:HEM801 4.4 49.4 1.0
CG B:HIS486 4.5 56.0 1.0
C4D B:HEM801 4.5 38.3 1.0
NB B:HEM801 4.5 41.6 1.0
CG B:HIS537 4.6 41.1 1.0
NA B:HEM801 4.6 39.6 1.0
OE1 B:GLU490 4.7 69.9 1.0
O B:HOH908 4.7 69.4 1.0
C2D B:HEM801 4.8 39.0 1.0
CHC B:HEM801 4.9 48.5 1.0
C4B B:HEM801 4.9 43.5 1.0
C B:GLY534 5.0 52.9 1.0
C3C B:HEM801 5.0 46.5 1.0
ND1 B:HIS538 5.0 35.4 1.0
C3D B:HEM801 5.0 38.0 1.0

Iron binding site 6 out of 6 in 28pn

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Iron binding site 6 out of 6 in the Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryoem Structure of Native Quinol Dependent Nitric Oxide Reductase at pH 8.0 on Gold Grid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe804

b:44.4
occ:1.00
 FE B:HEM804 0.0 44.4 1.0
NE2 B:HIS331 2.0 29.1 1.0
NC B:HEM804 2.1 29.1 1.0
NB B:HEM804 2.1 29.1 1.0
NA B:HEM804 2.1 30.3 1.0
ND B:HEM804 2.1 26.1 1.0
NE2 B:HIS631 2.6 23.5 1.0
CE1 B:HIS331 2.9 26.5 1.0
CD2 B:HIS331 3.0 24.9 1.0
C1D B:HEM804 3.1 25.9 1.0
C4C B:HEM804 3.1 25.0 1.0
C1B B:HEM804 3.1 29.6 1.0
C4A B:HEM804 3.1 25.5 1.0
C1A B:HEM804 3.1 26.6 1.0
C4D B:HEM804 3.1 24.2 1.0
C1C B:HEM804 3.1 27.5 1.0
C4B B:HEM804 3.1 28.8 1.0
CD2 B:HIS631 3.3 22.5 1.0
CHD B:HEM804 3.4 23.2 1.0
CHB B:HEM804 3.4 26.8 1.0
CHA B:HEM804 3.5 21.3 1.0
CHC B:HEM804 3.5 28.8 1.0
CE1 B:HIS631 3.7 27.9 1.0
ND1 B:HIS331 4.0 32.7 1.0
CG B:HIS331 4.1 29.9 1.0
C2D B:HEM804 4.3 28.7 1.0
C3D B:HEM804 4.3 27.4 1.0
C3A B:HEM804 4.3 25.1 1.0
C3C B:HEM804 4.3 26.9 1.0
C2A B:HEM804 4.3 26.6 1.0
C2B B:HEM804 4.3 31.2 1.0
C2C B:HEM804 4.3 26.1 1.0
C3B B:HEM804 4.3 29.2 1.0
CG B:HIS631 4.5 22.2 1.0
ND1 B:HIS631 4.7 29.1 1.0
NE2 B:GLN296 4.8 31.6 1.0

Reference:

F.T.Khaja, A.Mboukou, L.P.Aspinall, C.E.Hawksworth, R.R.Eady, S.V.Antonyuk, S.P.Muench, S.S.Hasnain. Cryoem Structures of Native Quinol-Dependent Nitric Oxide Reductase in Resting and Quinol-Bound States. Acs Bio Med Chem Au V. 6 145 2026.
ISSN: ESSN 2694-2437
PubMed: 42006251
DOI: 10.1021/ACSBIOMEDCHEMAU.5C00245
Page generated: Sun Oct 4 09:43:21 2026

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