Iron in PDB 4m4a: Human Hemoglobin Nitromethane Modified

The structure of Human Hemoglobin Nitromethane Modified, PDB code: 4m4a was solved by J.Yi, Y.Guan, 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)	21.40 / 2.05
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	53.573, 53.573, 191.870, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 28

The binding sites of Iron atom in the Human Hemoglobin Nitromethane Modified (pdb code 4m4a). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Hemoglobin Nitromethane Modified, PDB code: 4m4a:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Hemoglobin Nitromethane 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 Nitromethane Modified within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:26.2 occ:1.00 FE A:HEM201 0.0 26.2 1.0 NA A:HEM201 2.0 26.0 1.0 N A:NSM202 2.0 25.9 1.0 ND A:HEM201 2.0 26.1 1.0 NC A:HEM201 2.1 22.3 1.0 NB A:HEM201 2.1 21.2 1.0 NE2 A:HIS87 2.1 28.1 1.0 O1 A:NSM202 2.7 25.9 1.0 CE1 A:HIS87 3.0 25.9 1.0 C4D A:HEM201 3.0 28.6 1.0 C1A A:HEM201 3.0 26.9 1.0 C4A A:HEM201 3.0 23.5 1.0 C1D A:HEM201 3.1 25.9 1.0 C4C A:HEM201 3.1 25.1 1.0 C1B A:HEM201 3.1 23.2 1.0 C1C A:HEM201 3.1 22.9 1.0 C1 A:NSM202 3.1 25.9 1.0 C4B A:HEM201 3.1 21.9 1.0 CD2 A:HIS87 3.2 27.9 1.0 CHA A:HEM201 3.4 24.9 1.0 CHB A:HEM201 3.4 23.6 1.0 CHD A:HEM201 3.4 24.1 1.0 CHC A:HEM201 3.5 25.1 1.0 ND1 A:HIS87 4.2 28.2 1.0 C2A A:HEM201 4.2 25.2 1.0 C3A A:HEM201 4.2 25.2 1.0 C3D A:HEM201 4.2 29.1 1.0 CG A:HIS87 4.3 27.5 1.0 C2D A:HEM201 4.3 24.3 1.0 C3C A:HEM201 4.3 23.2 1.0 C2C A:HEM201 4.3 23.2 1.0 C2B A:HEM201 4.3 22.9 1.0 C3B A:HEM201 4.4 24.1 1.0 NE2 A:HIS58 4.7 24.1 1.0

Iron binding site 2 out of 2 in the Human Hemoglobin Nitromethane 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 Nitromethane Modified within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:31.9 occ:1.00 FE B:HEM201 0.0 31.9 1.0 NA B:HEM201 2.0 31.4 1.0 N B:NSM202 2.0 32.1 1.0 ND B:HEM201 2.1 33.3 1.0 NB B:HEM201 2.1 31.2 1.0 NC B:HEM201 2.2 33.5 1.0 NE2 B:HIS92 2.2 28.9 1.0 O1 B:NSM202 2.7 32.1 1.0 C1A B:HEM201 3.0 32.1 1.0 C4D B:HEM201 3.0 34.2 1.0 C1 B:NSM202 3.0 32.1 1.0 C4A B:HEM201 3.0 29.8 1.0 C1B B:HEM201 3.1 30.3 1.0 C4B B:HEM201 3.1 29.3 1.0 C1D B:HEM201 3.1 34.8 1.0 CD2 B:HIS92 3.1 28.3 1.0 C1C B:HEM201 3.1 31.0 1.0 C4C B:HEM201 3.1 31.0 1.0 CE1 B:HIS92 3.2 33.8 1.0 CHA B:HEM201 3.3 32.2 1.0 CHB B:HEM201 3.5 29.9 1.0 CHC B:HEM201 3.5 25.7 1.0 CHD B:HEM201 3.5 33.8 1.0 C2A B:HEM201 4.2 36.8 1.0 C3A B:HEM201 4.2 30.3 1.0 C3D B:HEM201 4.3 35.1 1.0 ND1 B:HIS92 4.3 30.7 1.0 CG B:HIS92 4.3 29.9 1.0 C2D B:HEM201 4.3 34.2 1.0 C2B B:HEM201 4.3 29.5 1.0 C3B B:HEM201 4.3 28.8 1.0 C2C B:HEM201 4.3 32.6 1.0 C3C B:HEM201 4.4 32.8 1.0 NE2 B:HIS63 4.6 33.3 1.0 CG2 B:VAL67 4.7 29.3 1.0

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