Iron in PDB 8wj1: Cryo-Em Structure of Human Haemoglobin in Oxy Form

The binding sites of Iron atom in the Cryo-Em Structure of Human Haemoglobin in Oxy Form (pdb code 8wj1). 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 Oxy Form, PDB code: 8wj1:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cryo-Em Structure of Human Haemoglobin in Oxy 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 Oxy Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:28.4 occ:1.00 FE A:HEM201 0.0 28.4 1.0 ND A:HEM201 2.0 31.4 1.0 NC A:HEM201 2.0 24.1 1.0 NA A:HEM201 2.0 27.9 1.0 O1 A:OXY202 2.0 51.6 1.0 NB A:HEM201 2.1 31.8 1.0 NE2 A:HIS87 2.1 26.9 1.0 C1D A:HEM201 2.9 28.1 1.0 C4C A:HEM201 3.0 30.2 1.0 C4D A:HEM201 3.0 28.4 1.0 C1A A:HEM201 3.0 30.9 1.0 C1C A:HEM201 3.0 33.9 1.0 C4B A:HEM201 3.1 29.6 1.0 C4A A:HEM201 3.1 31.2 1.0 C1B A:HEM201 3.1 29.1 1.0 O2 A:OXY202 3.1 84.0 1.0 CE1 A:HIS87 3.1 26.7 1.0 CD2 A:HIS87 3.2 24.4 1.0 CHA A:HEM201 3.4 31.7 1.0 CHD A:HEM201 3.4 29.7 1.0 CHC A:HEM201 3.5 33.7 1.0 CHB A:HEM201 3.5 31.9 1.0 NE2 A:HIS58 4.1 39.5 1.0 C2D A:HEM201 4.2 33.1 1.0 C2A A:HEM201 4.2 34.2 1.0 C3C A:HEM201 4.2 32.9 1.0 C3D A:HEM201 4.2 32.7 1.0 C2C A:HEM201 4.2 34.9 1.0 C3A A:HEM201 4.2 31.2 1.0 ND1 A:HIS87 4.3 25.8 1.0 C3B A:HEM201 4.3 36.9 1.0 CG A:HIS87 4.3 32.3 1.0 C2B A:HEM201 4.3 35.7 1.0 CE1 A:HIS58 4.5 47.2 1.0 CG2 A:VAL62 4.9 35.1 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Human Haemoglobin in Oxy 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 Oxy Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:38.5 occ:1.00 FE B:HEM201 0.0 38.5 1.0 ND B:HEM201 1.9 39.4 1.0 O1 B:OXY202 2.0 62.5 1.0 NA B:HEM201 2.0 36.3 1.0 NC B:HEM201 2.0 39.9 1.0 NE2 B:HIS92 2.1 43.3 1.0 NB B:HEM201 2.1 37.2 1.0 C1D B:HEM201 2.9 42.1 1.0 C4D B:HEM201 2.9 42.3 1.0 C1A B:HEM201 3.0 43.2 1.0 C4C B:HEM201 3.0 40.4 1.0 O2 B:OXY202 3.0 96.1 1.0 CE1 B:HIS92 3.0 46.5 1.0 C1C B:HEM201 3.0 45.5 1.0 C4A B:HEM201 3.0 36.7 1.0 C4B B:HEM201 3.1 35.7 1.0 C1B B:HEM201 3.1 36.8 1.0 CD2 B:HIS92 3.2 46.1 1.0 CHA B:HEM201 3.4 40.7 1.0 CHD B:HEM201 3.4 39.3 1.0 CHC B:HEM201 3.5 37.2 1.0 CHB B:HEM201 3.5 38.1 1.0 NE2 B:HIS63 4.1 46.1 1.0 C3D B:HEM201 4.1 49.8 1.0 C2D B:HEM201 4.1 48.4 1.0 C2A B:HEM201 4.2 43.4 1.0 ND1 B:HIS92 4.2 43.1 1.0 C3A B:HEM201 4.2 40.4 1.0 C3C B:HEM201 4.2 45.0 1.0 C2C B:HEM201 4.2 45.6 1.0 CG B:HIS92 4.3 47.8 1.0 C2B B:HEM201 4.4 38.8 1.0 C3B B:HEM201 4.4 38.3 1.0 CG2 B:VAL67 4.5 49.4 1.0 CE1 B:HIS63 4.6 59.3 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