Iron in PDB 1aom: Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase

The structure of Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase, PDB code: 1aom was solved by P.A.Williams, V.Fulop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	106.700, 60.600, 100.100, 90.00, 112.30, 90.00
R / Rfree (%)	18.1 / 20

The binding sites of Iron atom in the Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase (pdb code 1aom). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase, PDB code: 1aom:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:11.1 occ:1.00 FE A:DHE602 0.0 11.1 1.0 NE2 A:HIS200 2.0 14.4 1.0 N A:2NO603 2.0 19.2 1.0 NB A:DHE602 2.1 16.3 1.0 NC A:DHE602 2.1 14.6 1.0 ND A:DHE602 2.1 12.7 1.0 NA A:DHE602 2.1 13.9 1.0 O2 A:2NO603 2.8 22.7 1.0 O1 A:2NO603 2.8 24.8 1.0 CE1 A:HIS200 2.9 13.7 1.0 CD2 A:HIS200 3.0 12.6 1.0 C1C A:DHE602 3.0 15.7 1.0 C1B A:DHE602 3.0 17.2 1.0 C4B A:DHE602 3.1 17.8 1.0 C4A A:DHE602 3.1 14.9 1.0 C4C A:DHE602 3.1 13.7 1.0 C4D A:DHE602 3.1 10.9 1.0 C1D A:DHE602 3.1 11.7 1.0 C1A A:DHE602 3.1 13.8 1.0 CHC A:DHE602 3.3 16.5 1.0 CHB A:DHE602 3.4 16.4 1.0 CHA A:DHE602 3.4 12.5 1.0 CHD A:DHE602 3.4 12.9 1.0 ND1 A:HIS200 4.1 13.3 1.0 CG A:HIS200 4.1 13.2 1.0 C3D A:DHE602 4.3 10.7 1.0 C2D A:DHE602 4.3 10.4 1.0 C2A A:DHE602 4.3 13.2 1.0 C3A A:DHE602 4.3 14.9 1.0 C2B A:DHE602 4.3 18.5 1.0 C2C A:DHE602 4.3 17.5 1.0 C3B A:DHE602 4.4 18.1 1.0 C3C A:DHE602 4.4 14.9 1.0 O2C A:DHE602 4.8 17.2 1.0 O2B A:DHE602 4.9 24.8 1.0 O A:HOH620 5.0 13.3 1.0

Iron binding site 2 out of 3 in the Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:16.9 occ:1.00 FE B:HEM601 0.0 16.9 1.0 NB B:HEM601 1.9 16.6 1.0 ND B:HEM601 2.0 20.3 1.0 NA B:HEM601 2.0 18.4 1.0 NE2 B:HIS17 2.0 19.3 1.0 NC B:HEM601 2.0 18.3 1.0 NE2 B:HIS69 2.0 18.5 1.0 CE1 B:HIS17 2.8 18.6 1.0 CE1 B:HIS69 2.9 15.9 1.0 C4B B:HEM601 3.0 17.1 1.0 C4D B:HEM601 3.0 20.9 1.0 C1B B:HEM601 3.0 17.8 1.0 C1D B:HEM601 3.0 20.2 1.0 C1A B:HEM601 3.0 20.9 1.0 C1C B:HEM601 3.0 17.4 1.0 C4A B:HEM601 3.0 18.7 1.0 C4C B:HEM601 3.0 19.0 1.0 CD2 B:HIS69 3.1 15.9 1.0 CD2 B:HIS17 3.1 21.6 1.0 CHC B:HEM601 3.4 15.9 1.0 CHA B:HEM601 3.4 21.2 1.0 CHB B:HEM601 3.4 17.5 1.0 CHD B:HEM601 3.4 19.3 1.0 ND1 B:HIS17 4.0 21.3 1.0 ND1 B:HIS69 4.1 16.6 1.0 CG B:HIS17 4.2 23.6 1.0 CG B:HIS69 4.2 15.1 1.0 C3B B:HEM601 4.2 15.9 1.0 C2B B:HEM601 4.2 16.2 1.0 C3D B:HEM601 4.2 21.8 1.0 C2D B:HEM601 4.2 21.6 1.0 C2A B:HEM601 4.3 19.9 1.0 C3A B:HEM601 4.3 17.9 1.0 C3C B:HEM601 4.3 18.4 1.0 C2C B:HEM601 4.3 16.8 1.0 CE1 B:PHE97 4.9 22.9 1.0

Iron binding site 3 out of 3 in the Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Substrate and Product Bound to Cytochrome CD1 Nitrite Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:10.6 occ:1.00 FE B:DHE602 0.0 10.6 1.0 N B:NO603 2.0 16.9 1.0 NE2 B:HIS200 2.0 12.9 1.0 NB B:DHE602 2.1 13.9 1.0 ND B:DHE602 2.1 11.0 1.0 NA B:DHE602 2.1 12.4 1.0 NC B:DHE602 2.1 13.4 1.0 CE1 B:HIS200 2.8 11.1 1.0 C1B B:DHE602 3.0 15.2 1.0 O B:NO603 3.1 21.2 1.0 C1C B:DHE602 3.1 15.4 1.0 C4A B:DHE602 3.1 13.9 1.0 C4B B:DHE602 3.1 14.7 1.0 C1D B:DHE602 3.1 12.9 1.0 C4C B:DHE602 3.1 14.2 1.0 C4D B:DHE602 3.1 10.7 1.0 C1A B:DHE602 3.1 13.1 1.0 CD2 B:HIS200 3.2 12.1 1.0 CHC B:DHE602 3.4 15.2 1.0 CHB B:DHE602 3.4 13.4 1.0 CHD B:DHE602 3.4 13.3 1.0 CHA B:DHE602 3.4 12.3 1.0 ND1 B:HIS200 4.0 11.3 1.0 OH B:TYR25 4.1 39.4 1.0 CG B:HIS200 4.2 11.1 1.0 C3A B:DHE602 4.3 12.1 1.0 C2A B:DHE602 4.3 12.3 1.0 C2D B:DHE602 4.3 11.0 1.0 C3D B:DHE602 4.3 10.6 1.0 C2B B:DHE602 4.3 15.1 1.0 C2C B:DHE602 4.3 15.1 1.0 C3B B:DHE602 4.4 14.9 1.0 C3C B:DHE602 4.4 13.7 1.0 CZ B:TYR25 4.9 41.0 1.0

P.A.Williams, V.Fulop, E.F.Garman, N.F.Saunders, S.J.Ferguson, J.Hajdu. Haem-Ligand Switching During Catalysis in Crystals of A Nitrogen-Cycle Enzyme. Nature V. 389 406 1997.
ISSN: ISSN 0028-0836
PubMed: 9311786
DOI: 10.1038/38775