Iron in PDB 9vic: Cryo-Em Structure of Human Haemoglobin in the R Conformation

The binding sites of Iron atom in the Cryo-Em Structure of Human Haemoglobin in the R Conformation (pdb code 9vic). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cryo-Em Structure of Human Haemoglobin in the R Conformation, PDB code: 9vic:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cryo-Em Structure of Human Haemoglobin in the R Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Human Haemoglobin in the R Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:30.6 occ:1.00 FE A:HEM201 0.0 30.6 1.0 NA A:HEM201 1.9 36.8 1.0 ND A:HEM201 2.0 31.2 1.0 NC A:HEM201 2.1 31.1 1.0 NB A:HEM201 2.1 30.5 1.0 NE2 A:HIS87 2.5 31.6 1.0 C A:CMO202 2.7 56.7 1.0 C1A A:HEM201 2.8 36.4 1.0 C4A A:HEM201 2.9 34.6 1.0 C4D A:HEM201 2.9 28.6 1.0 C1D A:HEM201 3.0 30.0 1.0 C4C A:HEM201 3.1 26.5 1.0 C1C A:HEM201 3.1 35.6 1.0 C1B A:HEM201 3.1 32.6 1.0 C4B A:HEM201 3.1 33.3 1.0 CHA A:HEM201 3.3 32.4 1.0 CE1 A:HIS87 3.3 35.8 1.0 CHD A:HEM201 3.4 26.7 1.0 CHB A:HEM201 3.4 29.1 1.0 CHC A:HEM201 3.5 34.5 1.0 O A:CMO202 3.6 86.9 1.0 CD2 A:HIS87 3.6 36.8 1.0 C2A A:HEM201 4.0 36.7 1.0 C3A A:HEM201 4.0 35.5 1.0 NE2 A:HIS58 4.1 42.6 1.0 C3D A:HEM201 4.1 35.8 1.0 C2D A:HEM201 4.2 38.2 1.0 C2C A:HEM201 4.3 32.7 1.0 C3C A:HEM201 4.3 30.8 1.0 C2B A:HEM201 4.3 34.6 1.0 C3B A:HEM201 4.4 34.7 1.0 ND1 A:HIS87 4.5 38.9 1.0 CE1 A:HIS58 4.6 50.3 1.0 CG A:HIS87 4.6 40.0 1.0 CG2 A:VAL62 4.8 39.1 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Human Haemoglobin in the R Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Human Haemoglobin in the R Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:38.9 occ:1.00 FE B:HEM201 0.0 38.9 1.0 ND B:HEM201 1.9 44.1 1.0 NA B:HEM201 2.0 41.5 1.0 NC B:HEM201 2.1 41.8 1.0 NB B:HEM201 2.1 38.3 1.0 NE2 B:HIS92 2.3 44.5 1.0 C B:CMO202 2.7 57.3 1.0 C4D B:HEM201 2.9 43.1 1.0 C1D B:HEM201 2.9 43.5 1.0 C1A B:HEM201 3.0 42.2 1.0 C4C B:HEM201 3.0 42.0 1.0 C1B B:HEM201 3.1 37.8 1.0 C1C B:HEM201 3.1 41.0 1.0 C4A B:HEM201 3.1 39.6 1.0 C4B B:HEM201 3.1 41.3 1.0 CE1 B:HIS92 3.2 39.8 1.0 CD2 B:HIS92 3.3 42.8 1.0 CHA B:HEM201 3.3 43.8 1.0 CHD B:HEM201 3.4 38.1 1.0 O B:CMO202 3.4 73.7 1.0 CHC B:HEM201 3.5 40.0 1.0 CHB B:HEM201 3.5 36.9 1.0 C2D B:HEM201 4.1 49.9 1.0 C3D B:HEM201 4.2 54.6 1.0 NE2 B:HIS63 4.2 53.5 1.0 C2A B:HEM201 4.3 46.3 1.0 C3C B:HEM201 4.3 48.3 1.0 C3A B:HEM201 4.3 43.7 1.0 C2C B:HEM201 4.3 44.5 1.0 C2B B:HEM201 4.3 43.0 1.0 ND1 B:HIS92 4.3 43.9 1.0 C3B B:HEM201 4.4 38.6 1.0 CG B:HIS92 4.4 41.9 1.0 CG2 B:VAL67 4.4 51.0 1.0 CE1 B:HIS63 4.7 57.1 1.0

K.Takahashi, Y.Lee, T.Nishizawa, J.R.H.Tame. Conformational Analysis of Liganded Human Hemoglobin By Cryo Electron Microscopy Biorxiv 2025.
ISSN: ISSN 2692-8205
DOI: 10.1101/2025.07.07.661630