Iron in PDB 8zgo: Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis

All present enzymatic activity of Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis:
1.7.99.7;

The structure of Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Iron atom in the Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis (pdb code 8zgo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis, PDB code: 8zgo:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis


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 Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:96.7 occ:1.00 FE A:HEM801 0.0 96.7 1.0 ND A:HEM801 1.9 74.5 1.0 NA A:HEM801 2.0 69.8 1.0 NB A:HEM801 2.1 75.1 1.0 NC A:HEM801 2.1 62.3 1.0 NE2 A:HIS635 2.2 83.8 1.0 NE2 A:HIS335 2.4 56.3 1.0 C4D A:HEM801 2.9 69.4 1.0 C1D A:HEM801 2.9 69.4 1.0 C1A A:HEM801 3.0 64.9 1.0 C4A A:HEM801 3.0 65.6 1.0 C1B A:HEM801 3.0 69.4 1.0 C4C A:HEM801 3.1 63.1 1.0 CE1 A:HIS635 3.1 85.0 1.0 C4B A:HEM801 3.1 69.1 1.0 C1C A:HEM801 3.1 66.5 1.0 CD2 A:HIS635 3.2 64.4 1.0 CD2 A:HIS335 3.2 61.5 1.0 CHA A:HEM801 3.4 66.9 1.0 CHD A:HEM801 3.4 61.6 1.0 CE1 A:HIS335 3.4 64.2 1.0 CHB A:HEM801 3.4 66.6 1.0 CHC A:HEM801 3.5 64.8 1.0 C3D A:HEM801 4.1 66.0 1.0 C2D A:HEM801 4.1 70.0 1.0 ND1 A:HIS635 4.2 80.7 1.0 C2A A:HEM801 4.2 62.3 1.0 C3A A:HEM801 4.2 64.4 1.0 C2B A:HEM801 4.3 67.5 1.0 CG A:HIS635 4.3 58.5 1.0 C3C A:HEM801 4.3 66.9 1.0 C3B A:HEM801 4.3 67.8 1.0 C2C A:HEM801 4.3 69.9 1.0 CG A:HIS335 4.4 58.8 1.0 ND1 A:HIS335 4.5 71.4 1.0 NH2 A:ARG724 4.8 93.6 1.0 NE2 A:GLN294 4.9 77.2 1.0 O A:HOH927 4.9 30.0 1.0

Iron binding site 2 out of 3 in the Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis


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 Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe802 b:101.8 occ:1.00 FE A:HEM802 0.0 101.8 1.0 ND A:HEM802 1.9 85.1 1.0 NA A:HEM802 2.0 73.0 1.0 NC A:HEM802 2.1 84.7 1.0 NB A:HEM802 2.1 87.0 1.0 NE2 A:HIS633 2.2 73.3 1.0 C4D A:HEM802 2.9 79.5 1.0 C1D A:HEM802 2.9 81.2 1.0 C1A A:HEM802 3.0 78.3 1.0 C4A A:HEM802 3.0 75.4 1.0 C4C A:HEM802 3.0 85.2 1.0 C1B A:HEM802 3.1 83.1 1.0 C4B A:HEM802 3.1 85.7 1.0 C1C A:HEM802 3.1 80.6 1.0 CD2 A:HIS633 3.2 64.8 1.0 CE1 A:HIS633 3.2 77.2 1.0 CHA A:HEM802 3.3 82.6 1.0 CHD A:HEM802 3.4 83.7 1.0 CHB A:HEM802 3.5 82.6 1.0 CHC A:HEM802 3.5 80.7 1.0 OE2 A:GLU494 3.6 98.1 1.0 FE A:FE803 3.6 125.3 1.0 OE1 A:GLU494 4.1 97.6 1.0 C3D A:HEM802 4.1 73.3 1.0 C2D A:HEM802 4.1 73.6 1.0 C2A A:HEM802 4.1 75.0 1.0 CD A:GLU494 4.2 97.2 1.0 C3A A:HEM802 4.2 73.7 1.0 C3C A:HEM802 4.2 85.5 1.0 C2C A:HEM802 4.3 82.9 1.0 C2B A:HEM802 4.3 75.8 1.0 C3B A:HEM802 4.3 79.1 1.0 CG A:HIS633 4.3 63.9 1.0 ND1 A:HIS633 4.3 70.7 1.0 CE1 A:HIS542 4.6 74.8 1.0 NE2 A:HIS541 4.8 84.2 1.0 NE2 A:HIS542 4.9 71.0 1.0

Iron binding site 3 out of 3 in the Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis


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 Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe803 b:125.3 occ:1.00 NE2 A:HIS542 2.2 71.0 1.0 ND1 A:HIS490 2.3 74.0 1.0 NE2 A:HIS541 2.4 84.2 1.0 OE2 A:GLU494 2.6 98.1 1.0 CE1 A:HIS542 2.9 74.8 1.0 CE1 A:HIS490 2.9 73.4 1.0 OE1 A:GLU494 3.0 97.6 1.0 CD A:GLU494 3.1 97.2 1.0 CE1 A:HIS541 3.1 80.7 1.0 CD2 A:HIS542 3.3 70.1 1.0 CG A:HIS490 3.5 73.7 1.0 CD2 A:HIS541 3.5 84.3 1.0 FE A:HEM802 3.6 101.8 1.0 ND A:HEM802 3.7 85.1 1.0 NC A:HEM802 3.9 84.7 1.0 CB A:HIS490 4.0 74.2 1.0 C1D A:HEM802 4.0 81.2 1.0 ND1 A:HIS542 4.1 67.5 1.0 NE2 A:HIS490 4.2 78.2 1.0 C4C A:HEM802 4.2 85.2 1.0 CHD A:HEM802 4.3 83.7 1.0 CG A:HIS542 4.3 62.9 1.0 ND1 A:HIS541 4.3 82.1 1.0 C4D A:HEM802 4.3 79.5 1.0 NA A:HEM802 4.4 73.0 1.0 CD2 A:HIS490 4.4 67.4 1.0 NB A:HEM802 4.5 87.0 1.0 CG A:GLU494 4.5 92.5 1.0 CG A:HIS541 4.6 75.6 1.0 C1C A:HEM802 4.6 80.6 1.0 C2D A:HEM802 4.8 73.6 1.0 CA A:HIS490 4.9 69.0 1.0 CHA A:HEM802 4.9 82.6 1.0 O A:GLY538 4.9 95.5 1.0 C1A A:HEM802 4.9 78.3 1.0

C.C.Gopalasingam, Y.Shiro, T.Tosha. Cryoem Structure of Monomeric Quinol Dependent Nitric Oxide Reductase From Neisseria Meningitidis To Be Published.