Iron in PDB 9vib: Cryo-Em Structure of Human Haemoglobin in the R2 Conformation

The binding sites of Iron atom in the Cryo-Em Structure of Human Haemoglobin in the R2 Conformation (pdb code 9vib). 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 R2 Conformation, PDB code: 9vib:
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 R2 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 R2 Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:29.2 occ:1.00 FE A:HEM201 0.0 29.2 1.0 NA A:HEM201 2.0 31.8 1.0 ND A:HEM201 2.0 30.2 1.0 NC A:HEM201 2.1 28.2 1.0 NB A:HEM201 2.2 30.3 1.0 NE2 A:HIS87 2.3 28.7 1.0 C A:CMO202 2.8 49.4 1.0 C1A A:HEM201 2.9 32.3 1.0 C4D A:HEM201 3.0 28.6 1.0 C1D A:HEM201 3.0 30.2 1.0 C4A A:HEM201 3.0 28.8 1.0 C4C A:HEM201 3.1 26.4 1.0 C1C A:HEM201 3.1 28.1 1.0 C4B A:HEM201 3.1 29.5 1.0 C1B A:HEM201 3.2 29.2 1.0 CD2 A:HIS87 3.3 27.6 1.0 CE1 A:HIS87 3.3 28.8 1.0 CHA A:HEM201 3.4 26.8 1.0 CHD A:HEM201 3.4 29.4 1.0 CHC A:HEM201 3.4 31.3 1.0 CHB A:HEM201 3.5 28.0 1.0 O A:CMO202 3.6 82.3 1.0 NE2 A:HIS58 4.1 43.5 1.0 C2A A:HEM201 4.1 36.3 1.0 C3A A:HEM201 4.2 32.9 1.0 C3D A:HEM201 4.2 36.1 1.0 C2D A:HEM201 4.2 35.9 1.0 C2C A:HEM201 4.3 35.3 1.0 C3C A:HEM201 4.3 34.0 1.0 C2B A:HEM201 4.4 31.0 1.0 C3B A:HEM201 4.4 30.2 1.0 ND1 A:HIS87 4.4 30.9 1.0 CG A:HIS87 4.4 29.3 1.0 CE1 A:HIS58 4.7 48.9 1.0 CG2 A:VAL62 4.8 38.3 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Human Haemoglobin in the R2 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 R2 Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:34.1 occ:1.00 FE B:HEM201 0.0 34.1 1.0 ND B:HEM201 1.9 43.0 1.0 NA B:HEM201 2.0 37.7 1.0 NC B:HEM201 2.0 34.2 1.0 NB B:HEM201 2.1 36.7 1.0 NE2 B:HIS92 2.3 37.4 1.0 C B:CMO202 2.6 44.2 1.0 C4D B:HEM201 2.9 40.4 1.0 C1D B:HEM201 3.0 43.8 1.0 C1A B:HEM201 3.0 40.2 1.0 C4C B:HEM201 3.0 39.8 1.0 C1C B:HEM201 3.1 39.3 1.0 C1B B:HEM201 3.1 39.7 1.0 C4A B:HEM201 3.1 39.5 1.0 C4B B:HEM201 3.1 37.9 1.0 CE1 B:HIS92 3.3 39.6 1.0 CHA B:HEM201 3.3 38.9 1.0 O B:CMO202 3.3 80.7 1.0 CD2 B:HIS92 3.3 42.7 1.0 CHD B:HEM201 3.4 42.6 1.0 CHC B:HEM201 3.5 35.3 1.0 CHB B:HEM201 3.5 38.1 1.0 C3D B:HEM201 4.1 50.4 1.0 C2A B:HEM201 4.2 46.3 1.0 C2D B:HEM201 4.2 44.2 1.0 C3C B:HEM201 4.2 42.5 1.0 C3A B:HEM201 4.2 44.6 1.0 C2C B:HEM201 4.2 39.7 1.0 C2B B:HEM201 4.3 38.9 1.0 NE2 B:HIS63 4.3 51.6 1.0 C3B B:HEM201 4.3 39.1 1.0 ND1 B:HIS92 4.4 44.1 1.0 CG B:HIS92 4.5 48.4 1.0 CG2 B:VAL67 4.7 38.4 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