Iron in PDB 1out: Trout Hemoglobin I

The structure of Trout Hemoglobin I, PDB code: 1out was solved by J.Tame, J.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	63.280, 63.280, 312.740, 90.00, 90.00, 120.00
R / Rfree (%)	16.2 / 24.7

The binding sites of Iron atom in the Trout Hemoglobin I (pdb code 1out). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Trout Hemoglobin I, PDB code: 1out:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Trout Hemoglobin I


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Trout Hemoglobin I within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe143 b:21.2 occ:1.00 FE A:HEM143 0.0 21.2 1.0 ND A:HEM143 2.0 22.2 1.0 NC A:HEM143 2.0 16.7 1.0 NB A:HEM143 2.0 17.8 1.0 NA A:HEM143 2.1 21.9 1.0 NE2 A:HIS88 2.2 17.4 1.0 CE1 A:HIS88 3.0 19.5 1.0 C1C A:HEM143 3.0 14.4 1.0 C1D A:HEM143 3.0 23.1 1.0 C4D A:HEM143 3.1 22.2 1.0 C4C A:HEM143 3.1 16.9 1.0 C1A A:HEM143 3.1 26.1 1.0 C4B A:HEM143 3.1 16.4 1.0 C1B A:HEM143 3.1 18.2 1.0 C4A A:HEM143 3.1 19.2 1.0 CD2 A:HIS88 3.3 14.9 1.0 CHA A:HEM143 3.4 21.2 1.0 CHC A:HEM143 3.4 9.2 1.0 CHD A:HEM143 3.5 15.3 1.0 CHB A:HEM143 3.5 18.7 1.0 ND1 A:HIS88 4.2 17.2 1.0 NE2 A:HIS59 4.3 31.8 1.0 C3D A:HEM143 4.3 24.2 1.0 C2D A:HEM143 4.3 22.6 1.0 C2C A:HEM143 4.3 17.1 1.0 C3C A:HEM143 4.3 15.1 1.0 C3B A:HEM143 4.3 14.1 1.0 C2B A:HEM143 4.3 14.6 1.0 CD1 A:ILE63 4.3 28.5 1.0 C2A A:HEM143 4.3 29.6 1.0 C3A A:HEM143 4.3 26.2 1.0 CG A:HIS88 4.4 14.4 1.0 CG1 A:ILE63 4.4 17.5 1.0 CD1 A:LEU92 4.7 28.7 1.0 CE1 A:HIS59 4.7 36.3 1.0

Iron binding site 2 out of 2 in the Trout Hemoglobin I


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Trout Hemoglobin I within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe148 b:16.4 occ:1.00 FE B:HEM148 0.0 16.4 1.0 NB B:HEM148 2.0 18.3 1.0 NA B:HEM148 2.0 20.3 1.0 ND B:HEM148 2.0 20.7 1.0 NC B:HEM148 2.0 15.8 1.0 NE2 B:HIS92 2.1 13.1 1.0 CE1 B:HIS92 3.0 15.3 1.0 C4A B:HEM148 3.0 21.2 1.0 C1B B:HEM148 3.0 19.8 1.0 C1A B:HEM148 3.1 23.7 1.0 C4D B:HEM148 3.1 20.5 1.0 C1D B:HEM148 3.1 23.0 1.0 C4B B:HEM148 3.1 21.8 1.0 C4C B:HEM148 3.1 14.3 1.0 C1C B:HEM148 3.1 16.9 1.0 CD2 B:HIS92 3.2 8.3 1.0 CHB B:HEM148 3.4 21.8 1.0 CHD B:HEM148 3.4 18.6 1.0 CHC B:HEM148 3.5 22.0 1.0 CHA B:HEM148 3.5 20.5 1.0 CG2 B:VAL67 4.1 27.4 1.0 NE2 B:HIS63 4.1 23.0 1.0 ND1 B:HIS92 4.2 15.0 1.0 C2B B:HEM148 4.3 20.8 1.0 C3B B:HEM148 4.3 21.9 1.0 C3D B:HEM148 4.3 23.8 1.0 C3A B:HEM148 4.3 21.6 1.0 C2A B:HEM148 4.3 27.1 1.0 C2D B:HEM148 4.3 22.2 1.0 CG B:HIS92 4.3 20.8 1.0 C3C B:HEM148 4.3 13.1 1.0 C2C B:HEM148 4.3 13.7 1.0 CE1 B:HIS63 4.7 25.7 1.0 CD1 B:LEU96 4.9 21.5 1.0

J.R.Tame, J.C.Wilson, R.E.Weber. The Crystal Structures of Trout Hb I in the Deoxy and Carbonmonoxy Forms. J.Mol.Biol. V. 259 749 1996.
ISSN: ISSN 0022-2836
PubMed: 8683580
DOI: 10.1006/JMBI.1996.0355