Iron in PDB 1hj4: Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex

All present enzymatic activity of Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex:
1.7.2.1; 1.7.99.1;

The structure of Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex, PDB code: 1hj4 was solved by T.Sjogren, J.Hajdu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	106.690, 60.900, 100.590, 90.00, 112.08, 90.00
R / Rfree (%)	20.2 / 22.6

The binding sites of Iron atom in the Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex (pdb code 1hj4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex, PDB code: 1hj4:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:30.3 occ:1.00 FE A:HEC601 0.0 30.3 1.0 ND A:HEC601 2.0 31.9 1.0 NC A:HEC601 2.0 30.8 1.0 NB A:HEC601 2.0 30.8 1.0 NA A:HEC601 2.0 31.9 1.0 NE2 A:HIS69 2.1 27.9 1.0 NE2 A:HIS17 2.4 58.3 1.0 CD2 A:HIS17 2.9 59.3 1.0 C1C A:HEC601 3.0 31.1 1.0 C1D A:HEC601 3.0 31.6 1.0 C4D A:HEC601 3.0 32.2 1.0 C4C A:HEC601 3.0 31.1 1.0 C4A A:HEC601 3.0 31.8 1.0 C4B A:HEC601 3.0 32.2 1.0 C1A A:HEC601 3.1 32.7 1.0 C1B A:HEC601 3.1 31.6 1.0 CE1 A:HIS69 3.1 29.1 1.0 CD2 A:HIS69 3.1 28.3 1.0 CHD A:HEC601 3.4 31.4 1.0 CHC A:HEC601 3.4 31.1 1.0 CHA A:HEC601 3.4 32.5 1.0 CHB A:HEC601 3.4 31.5 1.0 CE1 A:HIS17 3.6 59.0 1.0 ND1 A:HIS69 4.2 28.3 1.0 CG A:HIS69 4.2 28.6 1.0 CG A:HIS17 4.2 59.4 1.0 C3C A:HEC601 4.2 31.4 1.0 C2D A:HEC601 4.3 32.5 1.0 C2C A:HEC601 4.3 31.3 1.0 C3D A:HEC601 4.3 32.7 1.0 C3B A:HEC601 4.3 32.0 1.0 C2A A:HEC601 4.3 33.1 1.0 C3A A:HEC601 4.3 32.5 1.0 C2B A:HEC601 4.3 31.9 1.0 ND1 A:HIS17 4.5 59.4 1.0

Iron binding site 2 out of 4 in the Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:17.7 occ:1.00 FE A:DHE602 0.0 17.7 1.0 NE2 A:HIS200 1.8 15.6 1.0 NA A:DHE602 2.0 15.2 1.0 ND A:DHE602 2.0 15.4 1.0 NB A:DHE602 2.0 19.8 1.0 NC A:DHE602 2.0 17.4 1.0 OH A:TYR25 2.3 36.1 1.0 CE1 A:HIS200 2.8 15.5 1.0 CD2 A:HIS200 2.8 13.8 1.0 C1A A:DHE602 3.0 16.0 1.0 C4D A:DHE602 3.0 14.4 1.0 C1B A:DHE602 3.0 21.4 1.0 C4A A:DHE602 3.0 17.7 1.0 C4B A:DHE602 3.0 21.9 1.0 C1D A:DHE602 3.1 15.3 1.0 C1C A:DHE602 3.1 20.9 1.0 C4C A:DHE602 3.1 18.6 1.0 CZ A:TYR25 3.3 38.4 1.0 CHB A:DHE602 3.4 18.8 1.0 CHA A:DHE602 3.4 15.3 1.0 CHC A:DHE602 3.4 22.3 1.0 CHD A:DHE602 3.4 15.6 1.0 O A:HOH2005 3.8 29.5 1.0 ND1 A:HIS200 3.9 18.2 1.0 CG A:HIS200 3.9 17.0 1.0 CE1 A:TYR25 4.0 38.3 1.0 CE2 A:TYR25 4.1 38.3 1.0 C3A A:DHE602 4.2 15.2 1.0 C2A A:DHE602 4.2 15.7 1.0 C3B A:DHE602 4.3 23.6 1.0 C2B A:DHE602 4.3 22.4 1.0 C3D A:DHE602 4.3 13.9 1.0 C2D A:DHE602 4.3 14.0 1.0 C3C A:DHE602 4.3 19.5 1.0 C2C A:DHE602 4.3 21.3 1.0 CGB A:DHE602 4.8 23.2 1.0

Iron binding site 3 out of 4 in the Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:28.0 occ:1.00 FE B:HEC601 0.0 28.0 1.0 NB B:HEC601 2.0 27.9 1.0 ND B:HEC601 2.0 27.8 1.0 NC B:HEC601 2.0 28.3 1.0 NA B:HEC601 2.0 28.8 1.0 NE2 B:HIS69 2.3 29.1 1.0 SD B:MET106 2.3 25.8 1.0 C4B B:HEC601 3.0 27.8 1.0 C1C B:HEC601 3.0 28.4 1.0 C1B B:HEC601 3.0 27.2 1.0 C1D B:HEC601 3.0 30.8 1.0 C4D B:HEC601 3.0 30.9 1.0 C4C B:HEC601 3.0 29.2 1.0 C1A B:HEC601 3.1 30.0 1.0 C4A B:HEC601 3.1 28.6 1.0 CD2 B:HIS69 3.2 29.1 1.0 CE1 B:HIS69 3.3 30.7 1.0 CHC B:HEC601 3.4 28.3 1.0 CE B:MET106 3.4 29.0 1.0 CHD B:HEC601 3.4 29.1 1.0 CHB B:HEC601 3.4 28.6 1.0 CHA B:HEC601 3.4 30.3 1.0 CG B:MET106 3.6 29.9 1.0 CB B:MET106 4.1 32.9 1.0 C3B B:HEC601 4.2 27.9 1.0 C2B B:HEC601 4.3 27.9 1.0 C3C B:HEC601 4.3 29.2 1.0 C2C B:HEC601 4.3 29.5 1.0 C2D B:HEC601 4.3 31.4 1.0 C3D B:HEC601 4.3 32.1 1.0 C2A B:HEC601 4.3 29.9 1.0 C3A B:HEC601 4.3 30.0 1.0 ND1 B:HIS69 4.4 29.4 1.0 CG B:HIS69 4.4 28.7 1.0 CA B:MET106 4.7 35.8 1.0

Iron binding site 4 out of 4 in the Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome CD1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:17.7 occ:1.00 FE B:DHE602 0.0 17.7 1.0 NE2 B:HIS200 1.9 16.8 1.0 NB B:DHE602 2.0 20.7 1.0 NA B:DHE602 2.0 16.7 1.0 ND B:DHE602 2.0 17.0 1.0 NC B:DHE602 2.0 19.6 1.0 CE1 B:HIS200 2.9 15.7 1.0 CD2 B:HIS200 2.9 14.7 1.0 C1B B:DHE602 3.0 22.2 1.0 C4D B:DHE602 3.0 16.6 1.0 C4A B:DHE602 3.0 18.8 1.0 C4B B:DHE602 3.0 22.8 1.0 C1A B:DHE602 3.0 17.0 1.0 C1D B:DHE602 3.0 17.9 1.0 C1C B:DHE602 3.0 22.6 1.0 C4C B:DHE602 3.1 21.7 1.0 CHB B:DHE602 3.4 20.3 1.0 CHC B:DHE602 3.4 23.6 1.0 CHA B:DHE602 3.4 17.5 1.0 CHD B:DHE602 3.4 19.1 1.0 ND1 B:HIS200 4.0 16.8 1.0 CG B:HIS200 4.0 15.6 1.0 C3A B:DHE602 4.2 17.8 1.0 C2B B:DHE602 4.2 23.7 1.0 C3B B:DHE602 4.2 24.4 1.0 C2A B:DHE602 4.3 17.3 1.0 C2D B:DHE602 4.3 17.7 1.0 C3D B:DHE602 4.3 16.6 1.0 C3C B:DHE602 4.3 22.6 1.0 C2C B:DHE602 4.3 23.7 1.0 O2B B:DHE602 4.9 27.1 1.0 CGB B:DHE602 5.0 25.3 1.0

T.Sjogren, J.Hajdu. Structure of the Bound Dioxygen Species in the Cytochrome Oxidase Reaction of Cytochrome CD1 Nitrite Reductase. J. Biol. Chem. V. 276 13072 2001.
ISSN: ISSN 0021-9258
PubMed: 11278884
DOI: 10.1074/JBC.M011312200