Iron in PDB 4m4b: Human Hemoglobin Nitroethane Modified

The structure of Human Hemoglobin Nitroethane Modified, PDB code: 4m4b was solved by J.Yi, L.M.Thomas, G.B.Richter-Addo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.43 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	53.443, 53.443, 193.581, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 27

The binding sites of Iron atom in the Human Hemoglobin Nitroethane Modified (pdb code 4m4b). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Human Hemoglobin Nitroethane Modified, PDB code: 4m4b:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Human Hemoglobin Nitroethane Modified


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Hemoglobin Nitroethane Modified within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:38.8 occ:1.00 FE A:HEM201 0.0 38.8 1.0 ND A:HEM201 2.0 35.5 1.0 NA A:HEM201 2.0 33.1 1.0 NC A:HEM201 2.1 35.7 1.0 NB A:HEM201 2.1 33.2 1.0 NE2 A:HIS87 2.3 32.6 1.0 N A:NOE203 2.4 35.5 1.0 O1 A:NOE203 2.6 50.4 1.0 C4D A:HEM201 3.0 35.9 1.0 C1A A:HEM201 3.0 39.3 1.0 C1D A:HEM201 3.1 36.0 1.0 C4C A:HEM201 3.1 36.1 1.0 C4A A:HEM201 3.1 36.3 1.0 CD2 A:HIS87 3.1 31.7 1.0 C1C A:HEM201 3.1 36.0 1.0 C1 A:NOE203 3.2 44.6 1.0 C1B A:HEM201 3.2 35.1 1.0 C4B A:HEM201 3.2 33.1 1.0 CHA A:HEM201 3.4 34.6 1.0 CHD A:HEM201 3.4 35.7 1.0 CE1 A:HIS87 3.4 43.2 1.0 CHB A:HEM201 3.5 35.7 1.0 CHC A:HEM201 3.5 32.4 1.0 C2 A:NOE203 4.1 41.1 1.0 C3D A:HEM201 4.3 38.6 1.0 C2A A:HEM201 4.3 43.2 1.0 C2D A:HEM201 4.3 35.1 1.0 C3A A:HEM201 4.3 43.9 1.0 C3C A:HEM201 4.3 36.1 1.0 C2C A:HEM201 4.3 36.2 1.0 CG A:HIS87 4.3 32.5 1.0 C2B A:HEM201 4.4 36.7 1.0 C3B A:HEM201 4.4 32.1 1.0 NE2 A:HIS58 4.4 42.0 1.0 ND1 A:HIS87 4.5 34.9 1.0

Iron binding site 2 out of 3 in the Human Hemoglobin Nitroethane Modified


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Hemoglobin Nitroethane Modified within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:46.5 occ:0.50 FE B:HEM201 0.0 46.5 0.5 CMC B:HEM201 1.3 53.2 0.5 C2C B:HEM201 1.6 54.8 0.5 C1C B:HEM201 1.9 52.5 0.5 CHC B:HEM201 2.0 56.4 0.5 NB B:HEM201 2.1 50.9 0.5 NC B:HEM201 2.1 51.2 0.5 NA B:HEM201 2.1 54.6 0.5 ND B:HEM201 2.1 49.9 0.5 NE2 B:HIS92 2.9 58.5 1.0 C3C B:HEM201 2.9 52.2 0.5 C4B B:HEM201 3.0 52.0 0.5 C1B B:HEM201 3.1 53.8 0.5 C1C B:HEM201 3.1 53.5 0.5 C4C B:HEM201 3.1 52.8 0.5 C1A B:HEM201 3.1 54.0 0.5 C4A B:HEM201 3.1 55.9 0.5 C4D B:HEM201 3.1 54.9 0.5 C1D B:HEM201 3.1 52.4 0.5 CD2 B:HIS92 3.2 52.8 1.0 NC B:HEM201 3.3 55.8 0.5 C4B B:HEM201 3.3 54.6 0.5 CHC B:HEM201 3.4 50.4 0.5 CHA B:HEM201 3.5 52.0 0.5 CHB B:HEM201 3.5 54.8 0.5 CHD B:HEM201 3.5 52.3 0.5 CBB B:HEM201 3.5 56.4 0.5 C4C B:HEM201 3.7 53.4 0.5 CAC B:HEM201 3.9 54.4 0.5 CE1 B:HIS92 4.1 58.3 1.0 C3B B:HEM201 4.2 57.1 0.5 C3B B:HEM201 4.2 53.2 0.5 C2B B:HEM201 4.2 49.6 0.5 CAB B:HEM201 4.3 57.9 0.5 C2C B:HEM201 4.3 56.2 0.5 C3C B:HEM201 4.3 54.8 0.5 C2A B:HEM201 4.3 57.2 0.5 C3A B:HEM201 4.3 58.0 0.5 NB B:HEM201 4.3 52.6 0.5 C3D B:HEM201 4.4 51.7 0.5 C2D B:HEM201 4.4 52.9 0.5 CG B:HIS92 4.5 52.4 1.0 CE1 B:HIS63 4.7 60.4 1.0 FE B:HEM201 4.9 53.3 0.5 ND1 B:HIS92 4.9 64.5 1.0 CZ B:PHE42 5.0 65.2 1.0

Iron binding site 3 out of 3 in the Human Hemoglobin Nitroethane Modified


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Hemoglobin Nitroethane Modified within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:53.3 occ:0.50 FE B:HEM201 0.0 53.3 0.5 CAD B:HEM201 0.9 53.9 0.5 C3D B:HEM201 1.2 51.7 0.5 C4D B:HEM201 1.8 54.9 0.5 ND B:HEM201 2.0 54.0 0.5 NC B:HEM201 2.0 55.8 0.5 NA B:HEM201 2.1 51.3 0.5 CHA B:HEM201 2.2 52.0 0.5 NB B:HEM201 2.2 52.6 0.5 CBD B:HEM201 2.3 58.8 0.5 C2D B:HEM201 2.7 52.9 0.5 C1D B:HEM201 3.0 56.6 0.5 C4C B:HEM201 3.0 53.4 0.5 C4D B:HEM201 3.0 57.8 0.5 C1C B:HEM201 3.1 52.5 0.5 C1A B:HEM201 3.1 51.8 0.5 ND B:HEM201 3.1 49.9 0.5 NE2 B:HIS63 3.2 65.6 1.0 C4A B:HEM201 3.2 52.5 0.5 CGD B:HEM201 3.2 53.3 0.5 O1D B:HEM201 3.2 51.1 0.5 C4B B:HEM201 3.2 54.6 0.5 C1B B:HEM201 3.3 57.7 0.5 CHD B:HEM201 3.3 51.4 0.5 CHA B:HEM201 3.4 53.0 0.5 C1D B:HEM201 3.5 52.4 0.5 CHC B:HEM201 3.5 56.4 0.5 C1A B:HEM201 3.6 54.0 0.5 CHB B:HEM201 3.6 57.8 0.5 CMD B:HEM201 3.8 50.0 0.5 CE1 B:HIS63 3.8 60.4 1.0 CD2 B:LEU91 4.0 53.9 1.0 C3C B:HEM201 4.2 52.2 0.5 C2D B:HEM201 4.2 55.2 0.5 C3D B:HEM201 4.2 53.9 0.5 C2C B:HEM201 4.2 54.8 0.5 C2A B:HEM201 4.3 55.8 0.5 CD2 B:HIS63 4.3 64.2 1.0 O2D B:HEM201 4.4 54.8 0.5 C3A B:HEM201 4.4 53.5 0.5 C3B B:HEM201 4.5 57.1 0.5 C2B B:HEM201 4.5 55.7 0.5 C2A B:HEM201 4.6 57.2 0.5 NA B:HEM201 4.6 54.6 0.5 CAA B:HEM201 4.7 55.6 0.5 CHD B:HEM201 4.8 52.3 0.5 NE2 B:HIS92 4.9 58.5 1.0 FE B:HEM201 4.9 46.5 0.5

J.Yi, G.Ye, L.M.Thomas, G.B.Richter-Addo. Degradation of Human Hemoglobin By Organic C-Nitroso Compounds. Chem.Commun.(Camb.) V. 49 11179 2013.
ISSN: ISSN 1359-7345
PubMed: 24149619
DOI: 10.1039/C3CC46174B