Iron in PDB 8wj2: Cryo-Em Structure of Human Haemoglobin in Deoxy Form

The binding sites of Iron atom in the Cryo-Em Structure of Human Haemoglobin in Deoxy Form (pdb code 8wj2). 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 Deoxy Form, PDB code: 8wj2:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cryo-Em Structure of Human Haemoglobin in Deoxy 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 Deoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:26.5 occ:1.00 FE A:HEM200 0.0 26.5 1.0 ND A:HEM200 2.0 33.0 1.0 NA A:HEM200 2.0 24.3 1.0 NC A:HEM200 2.0 26.0 1.0 NB A:HEM200 2.2 32.9 1.0 NE2 A:HIS87 2.2 31.9 1.0 C1A A:HEM200 3.0 25.3 1.0 C1D A:HEM200 3.0 24.3 1.0 C4D A:HEM200 3.0 30.6 1.0 C4C A:HEM200 3.0 32.5 1.0 C1C A:HEM200 3.1 36.1 1.0 C4B A:HEM200 3.1 29.6 1.0 CE1 A:HIS87 3.1 37.4 1.0 C4A A:HEM200 3.1 27.6 1.0 O A:HOH331 3.1 37.8 1.0 C1B A:HEM200 3.1 31.8 1.0 CD2 A:HIS87 3.3 33.8 1.0 CHA A:HEM200 3.4 32.0 1.0 CHD A:HEM200 3.4 25.4 1.0 CHC A:HEM200 3.5 32.0 1.0 CHB A:HEM200 3.6 29.5 1.0 C2A A:HEM200 4.2 28.0 1.0 C2D A:HEM200 4.2 33.5 1.0 C3D A:HEM200 4.2 34.9 1.0 C3C A:HEM200 4.3 35.2 1.0 C2C A:HEM200 4.3 36.7 1.0 C3A A:HEM200 4.3 26.1 1.0 ND1 A:HIS87 4.3 35.5 1.0 C3B A:HEM200 4.3 36.5 1.0 C2B A:HEM200 4.3 34.9 1.0 CE1 A:HIS58 4.4 33.2 1.0 CG A:HIS87 4.4 34.7 1.0 NE2 A:HIS58 4.5 28.0 1.0 CD1 A:LEU91 4.6 47.1 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Human Haemoglobin in Deoxy 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 Deoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:30.3 occ:1.00 FE B:HEM200 0.0 30.3 1.0 ND B:HEM200 1.9 37.3 1.0 NA B:HEM200 1.9 31.6 1.0 NC B:HEM200 2.1 30.0 1.0 NB B:HEM200 2.1 33.6 1.0 NE2 B:HIS92 2.3 29.8 1.0 C4D B:HEM200 2.9 36.0 1.0 C1D B:HEM200 2.9 34.5 1.0 C1A B:HEM200 2.9 36.9 1.0 C4A B:HEM200 3.0 35.6 1.0 C4C B:HEM200 3.0 31.7 1.0 C4B B:HEM200 3.0 34.2 1.0 C1B B:HEM200 3.1 30.6 1.0 C1C B:HEM200 3.1 33.1 1.0 CE1 B:HIS92 3.2 39.9 1.0 CD2 B:HIS92 3.3 35.7 1.0 CHA B:HEM200 3.3 33.0 1.0 CHD B:HEM200 3.4 28.8 1.0 CHB B:HEM200 3.5 31.7 1.0 CHC B:HEM200 3.5 31.7 1.0 O B:HOH302 3.7 70.1 1.0 CG2 B:VAL67 4.0 38.4 1.0 C3D B:HEM200 4.1 40.7 1.0 C2A B:HEM200 4.1 43.0 1.0 C3A B:HEM200 4.2 37.5 1.0 C2D B:HEM200 4.2 37.8 1.0 NE2 B:HIS63 4.2 38.7 1.0 C3C B:HEM200 4.3 37.6 1.0 C2B B:HEM200 4.3 30.2 1.0 C3B B:HEM200 4.3 32.4 1.0 C2C B:HEM200 4.3 34.8 1.0 ND1 B:HIS92 4.4 34.5 1.0 CG B:HIS92 4.4 35.8 1.0 CE1 B:HIS63 4.5 46.2 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