Iron in PDB 8wix: Cryo-Em Structure of Alligator Haemoglobin in Carbonmonoxy Form

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

Iron binding site 1 out of 2 in the Cryo-Em Structure of Alligator 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 Alligator Haemoglobin in Carbonmonoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:34.7 occ:1.00 FE A:HEM201 0.0 34.7 1.0 ND A:HEM201 1.9 35.7 1.0 NA A:HEM201 2.0 31.7 1.0 C A:CMO202 2.0 72.0 1.0 NC A:HEM201 2.1 32.8 1.0 NB A:HEM201 2.1 39.1 1.0 NE2 A:HIS87 2.2 39.4 1.0 C4D A:HEM201 2.9 41.3 1.0 C1D A:HEM201 2.9 34.0 1.0 C1A A:HEM201 2.9 32.2 1.0 O A:CMO202 3.0 70.8 1.0 C4A A:HEM201 3.0 33.6 1.0 C4B A:HEM201 3.0 41.4 1.0 C4C A:HEM201 3.0 35.6 1.0 C1B A:HEM201 3.0 33.4 1.0 C1C A:HEM201 3.1 43.1 1.0 CD2 A:HIS87 3.1 42.1 1.0 CE1 A:HIS87 3.2 44.0 1.0 CHA A:HEM201 3.3 40.3 1.0 CHD A:HEM201 3.4 37.7 1.0 CHB A:HEM201 3.5 29.1 1.0 CHC A:HEM201 3.5 42.0 1.0 C3D A:HEM201 4.1 42.0 1.0 C2D A:HEM201 4.1 39.0 1.0 C2A A:HEM201 4.1 35.3 1.0 NE2 A:HIS58 4.2 40.2 1.0 C3A A:HEM201 4.2 38.1 1.0 ND1 A:HIS87 4.3 48.3 1.0 C2B A:HEM201 4.3 36.1 1.0 C3B A:HEM201 4.3 38.8 1.0 C3C A:HEM201 4.3 39.0 1.0 CG A:HIS87 4.3 48.3 1.0 C2C A:HEM201 4.3 43.4 1.0 CE1 A:HIS58 4.7 46.3 1.0 CG2 A:VAL62 4.9 40.3 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Alligator 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 Alligator Haemoglobin in Carbonmonoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:36.8 occ:1.00 FE B:HEM201 0.0 36.8 1.0 ND B:HEM201 1.9 39.6 1.0 C B:CMO202 2.0 99.7 1.0 NA B:HEM201 2.0 35.5 1.0 NC B:HEM201 2.0 35.1 1.0 NB B:HEM201 2.1 36.9 1.0 NE2 B:HIS92 2.3 39.5 1.0 C1D B:HEM201 2.9 34.7 1.0 C4D B:HEM201 3.0 39.8 1.0 C1A B:HEM201 3.0 38.9 1.0 C4C B:HEM201 3.0 37.7 1.0 C4B B:HEM201 3.0 37.9 1.0 C4A B:HEM201 3.1 34.4 1.0 C1B B:HEM201 3.1 33.3 1.0 C1C B:HEM201 3.1 39.4 1.0 O B:CMO202 3.1 89.8 1.0 CE1 B:HIS92 3.2 46.0 1.0 CHD B:HEM201 3.4 34.5 1.0 CHA B:HEM201 3.4 41.1 1.0 CD2 B:HIS92 3.4 48.2 1.0 CHC B:HEM201 3.5 36.7 1.0 CHB B:HEM201 3.5 30.0 1.0 C2A B:HEM201 4.2 47.2 1.0 C2D B:HEM201 4.2 46.5 1.0 C3D B:HEM201 4.2 41.8 1.0 C3A B:HEM201 4.2 38.9 1.0 C3C B:HEM201 4.2 44.5 1.0 C2C B:HEM201 4.3 38.8 1.0 C2B B:HEM201 4.3 38.9 1.0 C3B B:HEM201 4.3 42.2 1.0 NE2 B:HIS63 4.4 43.7 1.0 ND1 B:HIS92 4.4 43.3 1.0 CG2 B:VAL67 4.5 42.0 1.0 CG B:HIS92 4.5 45.6 1.0 CE1 B:HIS63 4.9 46.5 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