Iron in PDB 3pia: 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: 3pia 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)	37.06 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.730, 73.210, 128.920, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.8

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 3pia). 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: 3pia:
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:13.1 occ:1.00 FE A:HEM142 0.0 13.1 1.0 C A:CMO143 1.8 9.2 1.0 ND A:HEM142 2.0 13.9 1.0 NC A:HEM142 2.0 11.4 1.0 NE2 A:HIS87 2.0 10.6 1.0 NA A:HEM142 2.1 14.7 1.0 NB A:HEM142 2.1 12.3 1.0 O A:CMO143 3.0 15.6 1.0 CE1 A:HIS87 3.0 9.6 1.0 C1D A:HEM142 3.0 13.8 1.0 C4A A:HEM142 3.0 13.2 1.0 C1C A:HEM142 3.0 11.1 1.0 C4C A:HEM142 3.0 12.4 1.0 CD2 A:HIS87 3.1 9.7 1.0 C1A A:HEM142 3.1 14.9 1.0 C4D A:HEM142 3.1 15.4 1.0 C4B A:HEM142 3.1 12.8 1.0 C1B A:HEM142 3.1 11.8 1.0 CHD A:HEM142 3.4 11.4 1.0 CHC A:HEM142 3.4 9.9 1.0 CHB A:HEM142 3.4 13.5 1.0 CHA A:HEM142 3.4 12.2 1.0 ND1 A:HIS87 4.1 11.6 1.0 CG A:HIS87 4.2 12.2 1.0 C3A A:HEM142 4.3 15.2 1.0 C3C A:HEM142 4.3 11.0 1.0 C2C A:HEM142 4.3 10.8 1.0 C2A A:HEM142 4.3 16.6 1.0 C2D A:HEM142 4.3 15.8 1.0 NE2 A:HIS58 4.3 16.9 1.0 C2B A:HEM142 4.3 10.8 1.0 C3D A:HEM142 4.3 13.4 1.0 C3B A:HEM142 4.3 12.2 1.0 CG2 A:VAL62 4.7 11.2 1.0 CE1 A:HIS58 5.0 16.0 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:15.9 occ:1.00 FE B:HEM147 0.0 15.9 1.0 C B:CMO148 1.8 15.4 1.0 NB B:HEM147 2.0 11.7 1.0 ND B:HEM147 2.0 14.7 1.0 NC B:HEM147 2.1 11.0 1.0 NA B:HEM147 2.1 13.7 1.0 NE2 B:HIS92 2.2 21.5 1.0 O B:CMO148 3.0 20.1 1.0 C4D B:HEM147 3.0 16.6 1.0 C1B B:HEM147 3.0 13.1 1.0 C1D B:HEM147 3.0 17.0 1.0 CD2 B:HIS92 3.1 16.4 1.0 C4B B:HEM147 3.1 12.4 1.0 C4C B:HEM147 3.1 11.1 1.0 C4A B:HEM147 3.1 16.3 1.0 C1C B:HEM147 3.1 8.8 1.0 C1A B:HEM147 3.1 16.6 1.0 CE1 B:HIS92 3.3 19.9 1.0 CHD B:HEM147 3.4 12.2 1.0 CHB B:HEM147 3.4 12.7 1.0 CHA B:HEM147 3.4 14.3 1.0 CHC B:HEM147 3.5 12.3 1.0 NE2 B:HIS63 4.2 27.2 1.0 C2B B:HEM147 4.2 15.1 1.0 C3D B:HEM147 4.2 17.0 1.0 C3B B:HEM147 4.3 14.2 1.0 C2D B:HEM147 4.3 12.9 1.0 CG B:HIS92 4.3 18.2 1.0 C3C B:HEM147 4.3 8.4 1.0 C2C B:HEM147 4.3 9.7 1.0 C3A B:HEM147 4.3 17.1 1.0 C2A B:HEM147 4.3 18.0 1.0 ND1 B:HIS92 4.4 18.3 1.0 CG2 B:VAL67 4.7 17.4 1.0 CE1 B:HIS63 4.9 27.8 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:13.3 occ:1.00 FE C:HEM142 0.0 13.3 1.0 C C:CMO143 1.9 12.6 1.0 NC C:HEM142 2.0 10.5 1.0 ND C:HEM142 2.0 12.2 1.0 NA C:HEM142 2.0 12.3 1.0 NE2 C:HIS87 2.0 12.6 1.0 NB C:HEM142 2.1 11.5 1.0 CD2 C:HIS87 3.0 8.2 1.0 C4C C:HEM142 3.0 13.9 1.0 O C:CMO143 3.0 17.6 1.0 C1C C:HEM142 3.0 9.8 1.0 C1D C:HEM142 3.0 12.6 1.0 C4A C:HEM142 3.0 15.7 1.0 C4D C:HEM142 3.1 12.9 1.0 C1A C:HEM142 3.1 15.1 1.0 C4B C:HEM142 3.1 12.5 1.0 CE1 C:HIS87 3.1 10.9 1.0 C1B C:HEM142 3.1 13.4 1.0 CHD C:HEM142 3.4 10.6 1.0 CHC C:HEM142 3.4 11.4 1.0 CHA C:HEM142 3.4 9.9 1.0 CHB C:HEM142 3.5 9.8 1.0 CG C:HIS87 4.1 11.7 1.0 ND1 C:HIS87 4.2 10.9 1.0 C3C C:HEM142 4.2 11.2 1.0 C2C C:HEM142 4.2 10.7 1.0 C2D C:HEM142 4.2 9.8 1.0 C3A C:HEM142 4.3 15.4 1.0 C2A C:HEM142 4.3 18.3 1.0 C3B C:HEM142 4.3 11.7 1.0 C3D C:HEM142 4.3 11.6 1.0 C2B C:HEM142 4.3 11.2 1.0 NE2 C:HIS58 4.3 17.6 1.0 CG2 C:VAL62 4.9 13.2 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:23.0 occ:1.00 FE D:HEM147 0.0 23.0 1.0 C D:CMO148 1.9 20.1 1.0 NB D:HEM147 2.1 21.2 1.0 ND D:HEM147 2.1 24.4 1.0 NC D:HEM147 2.1 20.9 1.0 NA D:HEM147 2.1 27.3 1.0 NE2 D:HIS92 2.2 26.2 1.0 O D:CMO148 3.0 25.9 1.0 C4C D:HEM147 3.1 21.5 1.0 CD2 D:HIS92 3.1 23.4 1.0 C1B D:HEM147 3.1 24.0 1.0 C1D D:HEM147 3.1 24.2 1.0 C4A D:HEM147 3.1 25.3 1.0 C4B D:HEM147 3.1 22.5 1.0 C1C D:HEM147 3.1 19.1 1.0 C1A D:HEM147 3.1 29.0 1.0 C4D D:HEM147 3.2 26.9 1.0 CE1 D:HIS92 3.2 25.4 1.0 CHD D:HEM147 3.4 21.4 1.0 CHB D:HEM147 3.4 23.0 1.0 CHA D:HEM147 3.5 28.6 1.0 CHC D:HEM147 3.5 19.8 1.0 CG D:HIS92 4.2 23.2 1.0 NE2 D:HIS63 4.2 31.1 1.0 ND1 D:HIS92 4.3 26.7 1.0 C3C D:HEM147 4.3 18.8 1.0 C2C D:HEM147 4.3 21.2 1.0 C2B D:HEM147 4.3 26.2 1.0 C3B D:HEM147 4.3 23.4 1.0 C3A D:HEM147 4.3 30.1 1.0 C2A D:HEM147 4.3 31.4 1.0 C2D D:HEM147 4.4 23.3 1.0 C3D D:HEM147 4.4 25.6 1.0 CG2 D:VAL67 4.7 19.5 1.0

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