Iron in PDB 3pi8: Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation

The structure of Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation, PDB code: 3pi8 was solved by V.S.Bhatt, T.J.Styslinger, N.Zhang, P.G.Wang, A.F.Palmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.06 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.977, 72.995, 128.483, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 28.1

The binding sites of Iron atom in the Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation (pdb code 3pi8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation, PDB code: 3pi8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:17.0 occ:1.00 FE A:HEM142 0.0 17.0 1.0 NE2 A:HIS87 2.0 17.3 1.0 NC A:HEM142 2.1 16.9 1.0 NA A:HEM142 2.1 18.6 1.0 ND A:HEM142 2.1 17.0 1.0 NB A:HEM142 2.1 17.8 1.0 C A:CMO143 2.8 30.7 1.0 CD2 A:HIS87 3.0 18.1 1.0 CE1 A:HIS87 3.0 17.7 1.0 C4C A:HEM142 3.1 17.1 1.0 C1C A:HEM142 3.1 17.0 1.0 C1A A:HEM142 3.1 19.1 1.0 C1D A:HEM142 3.1 17.5 1.0 C4D A:HEM142 3.1 17.9 1.0 C4A A:HEM142 3.1 19.1 1.0 C4B A:HEM142 3.1 17.2 1.0 C1B A:HEM142 3.1 17.5 1.0 CHD A:HEM142 3.4 17.2 1.0 CHA A:HEM142 3.4 17.8 1.0 CHC A:HEM142 3.5 16.6 1.0 CHB A:HEM142 3.5 19.0 1.0 O A:CMO143 3.8 32.1 1.0 ND1 A:HIS87 4.1 17.2 1.0 CG A:HIS87 4.2 18.9 1.0 C2C A:HEM142 4.3 17.4 1.0 C3C A:HEM142 4.3 16.8 1.0 C2A A:HEM142 4.3 19.9 1.0 C3A A:HEM142 4.3 19.1 1.0 C2D A:HEM142 4.3 17.7 1.0 C3B A:HEM142 4.4 17.2 1.0 C3D A:HEM142 4.4 17.5 1.0 C2B A:HEM142 4.4 17.5 1.0 NE2 A:HIS58 4.6 19.1 1.0 CE1 A:HIS58 5.0 19.7 1.0

Iron binding site 2 out of 4 in the Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:21.2 occ:1.00 FE B:HEM147 0.0 21.2 1.0 NB B:HEM147 2.0 21.4 1.0 NA B:HEM147 2.0 21.8 1.0 NE2 B:HIS92 2.1 24.2 1.0 ND B:HEM147 2.1 21.1 1.0 NC B:HEM147 2.1 20.6 1.0 CD2 B:HIS92 3.0 24.9 1.0 CE1 B:HIS92 3.1 24.4 1.0 C1A B:HEM147 3.1 22.4 1.0 C1B B:HEM147 3.1 22.1 1.0 C4B B:HEM147 3.1 21.2 1.0 C4A B:HEM147 3.1 21.9 1.0 C B:CMO148 3.1 47.1 1.0 C4D B:HEM147 3.1 22.1 1.0 C1C B:HEM147 3.1 20.4 1.0 C1D B:HEM147 3.2 21.7 1.0 C4C B:HEM147 3.2 20.3 1.0 CHA B:HEM147 3.4 21.8 1.0 CHB B:HEM147 3.4 21.7 1.0 CHC B:HEM147 3.4 20.3 1.0 CHD B:HEM147 3.5 21.1 1.0 ND1 B:HIS92 4.2 24.4 1.0 CG B:HIS92 4.2 26.0 1.0 O B:CMO148 4.2 47.6 1.0 C2B B:HEM147 4.3 21.9 1.0 C3B B:HEM147 4.3 21.9 1.0 C2A B:HEM147 4.3 23.5 1.0 C3A B:HEM147 4.3 22.3 1.0 C2C B:HEM147 4.3 19.9 1.0 C3C B:HEM147 4.4 20.4 1.0 C3D B:HEM147 4.4 22.6 1.0 C2D B:HEM147 4.4 21.6 1.0 NE2 B:HIS63 4.4 24.7 1.0 CG2 B:VAL67 4.9 21.5 1.0

Iron binding site 3 out of 4 in the Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:19.3 occ:1.00 FE C:HEM142 0.0 19.3 1.0 NA C:HEM142 2.1 20.5 1.0 NC C:HEM142 2.1 19.2 1.0 ND C:HEM142 2.1 19.6 1.0 NE2 C:HIS87 2.1 19.2 1.0 NB C:HEM142 2.1 19.8 1.0 C C:CMO143 2.9 30.9 1.0 CD2 C:HIS87 3.1 18.7 1.0 C4C C:HEM142 3.1 19.6 1.0 C4A C:HEM142 3.1 20.0 1.0 C1A C:HEM142 3.1 20.8 1.0 C1D C:HEM142 3.1 18.8 1.0 C4D C:HEM142 3.1 19.6 1.0 C1C C:HEM142 3.1 19.2 1.0 CE1 C:HIS87 3.1 17.7 1.0 C1B C:HEM142 3.1 19.8 1.0 C4B C:HEM142 3.1 19.4 1.0 CHD C:HEM142 3.4 19.4 1.0 CHA C:HEM142 3.4 19.7 1.0 CHB C:HEM142 3.5 19.5 1.0 CHC C:HEM142 3.5 19.4 1.0 O C:CMO143 4.0 32.0 1.0 ND1 C:HIS87 4.2 17.4 1.0 CG C:HIS87 4.2 19.3 1.0 C3A C:HEM142 4.3 20.6 1.0 C2A C:HEM142 4.3 21.6 1.0 C3C C:HEM142 4.3 18.6 1.0 C2C C:HEM142 4.3 18.6 1.0 C2D C:HEM142 4.3 18.6 1.0 C3D C:HEM142 4.3 18.8 1.0 C2B C:HEM142 4.4 19.1 1.0 C3B C:HEM142 4.4 19.8 1.0 NE2 C:HIS58 4.6 24.3 1.0

Iron binding site 4 out of 4 in the Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Site-Specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry As A Viable Alternative to Pegylation within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:31.0 occ:1.00 FE D:HEM147 0.0 31.0 1.0 NC D:HEM147 2.1 29.8 1.0 ND D:HEM147 2.1 31.3 1.0 NE2 D:HIS92 2.1 35.1 1.0 NA D:HEM147 2.1 31.7 1.0 NB D:HEM147 2.1 30.8 1.0 CD2 D:HIS92 3.0 35.4 1.0 C1D D:HEM147 3.1 31.2 1.0 C4C D:HEM147 3.1 29.6 1.0 C D:CMO148 3.1 47.0 1.0 C4D D:HEM147 3.1 31.9 1.0 C1C D:HEM147 3.1 29.2 1.0 CE1 D:HIS92 3.1 35.3 1.0 C1A D:HEM147 3.1 32.6 1.0 C4A D:HEM147 3.1 32.3 1.0 C1B D:HEM147 3.1 31.0 1.0 C4B D:HEM147 3.2 30.6 1.0 CHD D:HEM147 3.4 30.0 1.0 CHA D:HEM147 3.5 32.6 1.0 CHB D:HEM147 3.5 31.3 1.0 CHC D:HEM147 3.5 29.7 1.0 CG D:HIS92 4.2 35.8 1.0 ND1 D:HIS92 4.2 35.3 1.0 O D:CMO148 4.2 47.8 1.0 C3C D:HEM147 4.3 28.8 1.0 C2D D:HEM147 4.3 31.3 1.0 C2C D:HEM147 4.3 28.9 1.0 C3D D:HEM147 4.3 31.9 1.0 C3A D:HEM147 4.4 32.9 1.0 C2A D:HEM147 4.4 33.5 1.0 C2B D:HEM147 4.4 31.1 1.0 C3B D:HEM147 4.4 30.5 1.0 NE2 D:HIS63 4.5 32.3 1.0

V.S.Bhatt, T.J.Styslinger, N.Zhang, P.G.Wang, A.F.Palmer. N/A N/A.