Iron in PDB 8wj0: Cryo-Em Structure of Human Haemoglobin in Carbonmonoxy Form

The binding sites of Iron atom in the Cryo-Em Structure of Human Haemoglobin in Carbonmonoxy Form (pdb code 8wj0). 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 Carbonmonoxy Form, PDB code: 8wj0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cryo-Em Structure of Human Haemoglobin in Carbonmonoxy Form


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 Carbonmonoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:24.3 occ:1.00 FE A:HEM201 0.0 24.3 1.0 ND A:HEM201 1.9 26.0 1.0 C A:CMO202 1.9 64.8 1.0 NA A:HEM201 2.0 24.3 1.0 NC A:HEM201 2.0 24.5 1.0 NB A:HEM201 2.1 28.4 1.0 NE2 A:HIS87 2.1 23.6 1.0 C4D A:HEM201 2.9 26.2 1.0 C1D A:HEM201 2.9 25.9 1.0 C1A A:HEM201 3.0 29.2 1.0 C4C A:HEM201 3.0 25.2 1.0 C4A A:HEM201 3.0 27.0 1.0 O A:CMO202 3.0 40.2 1.0 C4B A:HEM201 3.1 29.9 1.0 C1B A:HEM201 3.1 25.8 1.0 C1C A:HEM201 3.1 33.4 1.0 CE1 A:HIS87 3.1 26.8 1.0 CD2 A:HIS87 3.2 25.3 1.0 CHD A:HEM201 3.4 25.4 1.0 CHA A:HEM201 3.4 27.4 1.0 CHB A:HEM201 3.5 24.6 1.0 CHC A:HEM201 3.5 30.5 1.0 C3D A:HEM201 4.2 30.9 1.0 C2A A:HEM201 4.2 31.7 1.0 C2D A:HEM201 4.2 29.8 1.0 C3A A:HEM201 4.2 28.9 1.0 NE2 A:HIS58 4.2 37.8 1.0 C3C A:HEM201 4.3 29.8 1.0 ND1 A:HIS87 4.3 27.1 1.0 C2C A:HEM201 4.3 30.3 1.0 C2B A:HEM201 4.3 29.0 1.0 C3B A:HEM201 4.3 30.3 1.0 CG A:HIS87 4.3 27.4 1.0 CG2 A:VAL62 4.9 36.0 1.0 CE1 A:HIS58 5.0 43.2 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Human Haemoglobin in Carbonmonoxy Form


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 Carbonmonoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:30.5 occ:1.00 FE B:HEM201 0.0 30.5 1.0 ND B:HEM201 1.9 37.0 1.0 NA B:HEM201 2.0 34.6 1.0 C B:CMO202 2.0 59.3 1.0 NC B:HEM201 2.0 31.7 1.0 NB B:HEM201 2.1 33.6 1.0 NE2 B:HIS92 2.2 37.8 1.0 C4D B:HEM201 2.9 36.4 1.0 C1D B:HEM201 3.0 38.7 1.0 C4C B:HEM201 3.0 35.3 1.0 C1C B:HEM201 3.0 37.1 1.0 C1A B:HEM201 3.0 35.0 1.0 C4B B:HEM201 3.0 32.5 1.0 C1B B:HEM201 3.0 34.9 1.0 C4A B:HEM201 3.0 36.1 1.0 O B:CMO202 3.1 54.2 1.0 CD2 B:HIS92 3.2 42.2 1.0 CE1 B:HIS92 3.2 39.0 1.0 CHC B:HEM201 3.4 34.8 1.0 CHA B:HEM201 3.4 38.0 1.0 CHD B:HEM201 3.4 35.4 1.0 CHB B:HEM201 3.5 33.9 1.0 C3C B:HEM201 4.2 43.6 1.0 C2C B:HEM201 4.2 39.0 1.0 C3D B:HEM201 4.2 45.2 1.0 C2A B:HEM201 4.2 41.6 1.0 C2D B:HEM201 4.2 41.3 1.0 C2B B:HEM201 4.2 35.4 1.0 C3A B:HEM201 4.2 40.3 1.0 C3B B:HEM201 4.2 35.7 1.0 ND1 B:HIS92 4.3 43.8 1.0 CG B:HIS92 4.3 44.0 1.0 NE2 B:HIS63 4.4 47.6 1.0 CG2 B:VAL67 4.7 36.8 1.0

K.Takahashi, Y.Lee, A.Fago, N.M.Bautista, J.F.Storz, A.Kawamoto, G.Kurisu, T.Nishizawa, J.R.H.Tame. The Unique Allosteric Property of Crocodilian Haemoglobin Elucidated By Cryo-Em. Nat Commun V. 15 6505 2024.
ISSN: ESSN 2041-1723
PubMed: 39090102
DOI: 10.1038/S41467-024-49947-X