Iron in PDB 1jeb: Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2)

The structure of Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2), PDB code: 1jeb was solved by R.D.Kidd, J.E.Russell, N.J.Watmough, E.N.Baker, T.Brittain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.10
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	84.921, 84.921, 104.523, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 24.9

The binding sites of Iron atom in the Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2) (pdb code 1jeb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2), PDB code: 1jeb:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:34.9 occ:1.00 FE A:HEM142 0.0 34.9 1.0 C A:CMO143 1.8 62.7 1.0 NA A:HEM142 2.0 34.7 1.0 NB A:HEM142 2.0 33.0 1.0 NC A:HEM142 2.0 32.3 1.0 ND A:HEM142 2.0 34.4 1.0 NE2 A:HIS87 2.3 33.8 1.0 O A:CMO143 2.8 62.4 1.0 C1A A:HEM142 3.0 35.8 1.0 C1B A:HEM142 3.0 33.0 1.0 C4D A:HEM142 3.0 35.1 1.0 C4B A:HEM142 3.0 31.8 1.0 C4A A:HEM142 3.0 35.3 1.0 C1C A:HEM142 3.1 31.8 1.0 C4C A:HEM142 3.1 32.0 1.0 C1D A:HEM142 3.1 33.8 1.0 CD2 A:HIS87 3.2 32.7 1.0 CE1 A:HIS87 3.3 34.2 1.0 CHA A:HEM142 3.3 35.8 1.0 CHB A:HEM142 3.4 33.6 1.0 CHC A:HEM142 3.4 32.4 1.0 CHD A:HEM142 3.4 33.5 1.0 C2A A:HEM142 4.3 37.0 1.0 C2B A:HEM142 4.3 32.5 1.0 C3B A:HEM142 4.3 31.7 1.0 C3A A:HEM142 4.3 36.0 1.0 C3C A:HEM142 4.3 31.7 1.0 C2C A:HEM142 4.3 32.0 1.0 C3D A:HEM142 4.3 35.0 1.0 C2D A:HEM142 4.3 34.5 1.0 CG A:HIS87 4.4 33.0 1.0 ND1 A:HIS87 4.4 34.0 1.0 CE1 A:HIS58 4.5 45.2 1.0 NE2 A:HIS58 4.6 44.5 1.0

Iron binding site 2 out of 4 in the Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:60.1 occ:1.00 FE B:HEM147 0.0 60.1 1.0 C B:CMO148 1.7 20.3 1.0 NA B:HEM147 2.0 61.0 1.0 NB B:HEM147 2.0 60.1 1.0 ND B:HEM147 2.0 60.7 1.0 NC B:HEM147 2.0 60.5 1.0 NE2 B:HIS92 2.5 75.2 1.0 O B:CMO148 2.7 22.2 1.0 C1A B:HEM147 3.0 61.0 1.0 C4D B:HEM147 3.0 61.6 1.0 C1B B:HEM147 3.0 60.0 1.0 C4B B:HEM147 3.1 59.9 1.0 C4A B:HEM147 3.1 60.9 1.0 C1C B:HEM147 3.1 59.8 1.0 C4C B:HEM147 3.1 60.2 1.0 C1D B:HEM147 3.1 61.2 1.0 CD2 B:HIS92 3.2 75.4 1.0 CHA B:HEM147 3.4 61.1 1.0 CHB B:HEM147 3.4 60.5 1.0 CHC B:HEM147 3.4 59.7 1.0 CHD B:HEM147 3.5 60.6 1.0 CE1 B:HIS92 3.7 75.6 1.0 C3B B:HEM147 4.3 59.8 1.0 C2B B:HEM147 4.3 59.9 1.0 C2A B:HEM147 4.3 61.8 1.0 C3D B:HEM147 4.3 62.4 1.0 C3A B:HEM147 4.3 61.6 1.0 NE2 B:HIS63 4.3 65.2 1.0 C3C B:HEM147 4.3 60.1 1.0 C2C B:HEM147 4.3 60.1 1.0 C2D B:HEM147 4.4 61.9 1.0 CG B:HIS92 4.5 75.3 1.0 CG2 B:VAL67 4.6 64.9 1.0 ND1 B:HIS92 4.7 75.4 1.0

Iron binding site 3 out of 4 in the Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:37.6 occ:1.00 FE C:HEM142 0.0 37.6 1.0 C C:CMO143 1.8 69.6 1.0 NA C:HEM142 2.0 38.2 1.0 NB C:HEM142 2.0 37.6 1.0 NC C:HEM142 2.0 37.2 1.0 ND C:HEM142 2.0 38.4 1.0 NE2 C:HIS87 2.2 42.9 1.0 O C:CMO143 2.9 68.6 1.0 C1A C:HEM142 3.0 38.2 1.0 C4D C:HEM142 3.0 38.0 1.0 C4B C:HEM142 3.0 36.8 1.0 C1B C:HEM142 3.0 37.3 1.0 C1C C:HEM142 3.1 37.8 1.0 C4A C:HEM142 3.1 37.5 1.0 C4C C:HEM142 3.1 37.1 1.0 CD2 C:HIS87 3.1 43.4 1.0 C1D C:HEM142 3.1 37.6 1.0 CE1 C:HIS87 3.2 44.0 1.0 CHA C:HEM142 3.3 38.0 1.0 CHC C:HEM142 3.4 37.4 1.0 CHB C:HEM142 3.4 38.1 1.0 CHD C:HEM142 3.5 37.2 1.0 C2A C:HEM142 4.3 38.8 1.0 ND1 C:HIS87 4.3 45.0 1.0 CG C:HIS87 4.3 44.3 1.0 C3A C:HEM142 4.3 37.9 1.0 C3B C:HEM142 4.3 37.6 1.0 C2B C:HEM142 4.3 37.6 1.0 C3D C:HEM142 4.3 38.9 1.0 C2C C:HEM142 4.3 37.2 1.0 C3C C:HEM142 4.3 36.4 1.0 C2D C:HEM142 4.4 37.7 1.0 CE1 C:HIS58 4.4 46.3 1.0 NE2 C:HIS58 4.6 45.3 1.0 CG2 C:VAL62 4.9 37.5 1.0

Iron binding site 4 out of 4 in the Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Chimeric Human/Mouse Carbonmonoxy Hemoglobin (Human ZETA2 / Mouse BETA2) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:33.3 occ:1.00 FE D:HEM147 0.0 33.3 1.0 C D:CMO148 1.9 43.2 1.0 NB D:HEM147 2.0 31.2 1.0 NA D:HEM147 2.0 33.3 1.0 ND D:HEM147 2.0 33.2 1.0 NC D:HEM147 2.0 32.0 1.0 NE2 D:HIS92 2.2 40.1 1.0 O D:CMO148 2.9 41.5 1.0 C4D D:HEM147 3.0 35.3 1.0 C1A D:HEM147 3.0 34.7 1.0 C4B D:HEM147 3.0 31.0 1.0 C1B D:HEM147 3.1 31.7 1.0 C1C D:HEM147 3.1 31.0 1.0 C4A D:HEM147 3.1 33.8 1.0 C4C D:HEM147 3.1 32.4 1.0 C1D D:HEM147 3.1 34.5 1.0 CE1 D:HIS92 3.1 39.4 1.0 CD2 D:HIS92 3.1 39.0 1.0 CHA D:HEM147 3.3 34.5 1.0 CHC D:HEM147 3.4 30.5 1.0 CHB D:HEM147 3.5 31.5 1.0 CHD D:HEM147 3.5 32.5 1.0 ND1 D:HIS92 4.2 39.5 1.0 C3B D:HEM147 4.3 31.8 1.0 C3D D:HEM147 4.3 37.0 1.0 C2A D:HEM147 4.3 37.2 1.0 CG D:HIS92 4.3 39.7 1.0 NE2 D:HIS63 4.3 40.6 1.0 C2B D:HEM147 4.3 31.2 1.0 C3A D:HEM147 4.3 35.6 1.0 C2D D:HEM147 4.3 35.0 1.0 C2C D:HEM147 4.3 32.9 1.0 C3C D:HEM147 4.3 32.9 1.0 CG2 D:VAL67 4.8 31.9 1.0 CE1 D:HIS63 4.9 41.5 1.0

R.D.Kidd, J.E.Russell, N.J.Watmough, E.N.Baker, T.Brittain. The Role of Beta Chains in the Control of the Hemoglobin Oxygen Binding Function: Chimeric Human/Mouse Proteins, Structure, and Function. Biochemistry V. 40 15669 2001.
ISSN: ISSN 0006-2960
PubMed: 11747442
DOI: 10.1021/BI011329F