Iron in PDB 5hy8: Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes

The structure of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes, PDB code: 5hy8 was solved by N.T.Saraswathi, N.S.Pannu, V.E.Syakhovich, A.Saurabh, S.B.Bokut, D.Moras, M.Ruff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	112.13 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	237.987, 59.267, 137.024, 90.00, 125.36, 90.00
R / Rfree (%)	20.3 / 24.4

The binding sites of Iron atom in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes (pdb code 5hy8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 10 binding sites of Iron where determined in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes, PDB code: 5hy8:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:34.8 occ:1.00 FE A:HEM201 0.0 34.8 1.0 NE2 A:HIS87 1.9 55.9 1.0 ND A:HEM201 1.9 40.1 1.0 O1 A:OXY202 2.0 46.5 1.0 NA A:HEM201 2.0 51.1 1.0 NB A:HEM201 2.1 41.6 1.0 NC A:HEM201 2.1 37.0 1.0 CE1 A:HIS87 2.8 56.9 1.0 C4D A:HEM201 2.9 39.4 1.0 C1D A:HEM201 2.9 42.2 1.0 CD2 A:HIS87 3.0 52.8 1.0 C1A A:HEM201 3.0 47.8 1.0 C4B A:HEM201 3.0 35.7 1.0 C1B A:HEM201 3.0 44.5 1.0 C4A A:HEM201 3.1 46.0 1.0 C1C A:HEM201 3.1 30.4 1.0 O2 A:OXY202 3.1 72.3 1.0 C4C A:HEM201 3.1 36.5 1.0 CHA A:HEM201 3.4 45.6 1.0 CHC A:HEM201 3.4 31.0 1.0 CHD A:HEM201 3.4 37.4 1.0 CHB A:HEM201 3.5 44.1 1.0 ND1 A:HIS87 4.0 56.5 1.0 CG A:HIS87 4.1 54.2 1.0 C3D A:HEM201 4.2 44.7 1.0 C2D A:HEM201 4.2 33.7 1.0 C2A A:HEM201 4.2 53.8 1.0 C3A A:HEM201 4.3 49.0 1.0 C2B A:HEM201 4.3 37.7 1.0 NE2 A:HIS58 4.3 65.5 1.0 C2C A:HEM201 4.3 35.6 1.0 C3B A:HEM201 4.3 35.7 1.0 C3C A:HEM201 4.3 32.1 1.0 CE1 A:HIS58 4.4 67.9 1.0 CG2 A:VAL62 4.8 64.0 1.0

Iron binding site 2 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:24.5 occ:1.00 FE B:HEM201 0.0 24.5 1.0 ND B:HEM201 1.9 25.5 1.0 NE2 B:HIS92 2.0 35.4 1.0 O1 B:OXY202 2.0 35.7 1.0 NA B:HEM201 2.0 30.6 1.0 NB B:HEM201 2.1 27.3 1.0 NC B:HEM201 2.1 25.9 1.0 O2 B:OXY202 2.3 56.0 1.0 CE1 B:HIS92 2.9 36.2 1.0 C4D B:HEM201 2.9 25.4 1.0 C1D B:HEM201 3.0 29.3 1.0 C1A B:HEM201 3.0 26.9 1.0 C4B B:HEM201 3.0 28.4 1.0 C1C B:HEM201 3.1 26.1 1.0 C1B B:HEM201 3.1 31.5 1.0 C4A B:HEM201 3.1 32.5 1.0 CD2 B:HIS92 3.1 35.5 1.0 C4C B:HEM201 3.1 26.0 1.0 CHA B:HEM201 3.3 24.7 1.0 CHC B:HEM201 3.4 24.1 1.0 CHB B:HEM201 3.5 35.2 1.0 CHD B:HEM201 3.5 25.7 1.0 ND1 B:HIS92 4.0 34.8 1.0 C3D B:HEM201 4.2 29.1 1.0 CG B:HIS92 4.2 34.5 1.0 C2A B:HEM201 4.2 33.4 1.0 C2D B:HEM201 4.2 26.7 1.0 C3A B:HEM201 4.3 35.6 1.0 C2B B:HEM201 4.3 28.7 1.0 C2C B:HEM201 4.3 26.2 1.0 NE2 B:HIS63 4.3 47.6 1.0 C3B B:HEM201 4.3 30.3 1.0 C3C B:HEM201 4.3 24.5 1.0 CG2 B:VAL67 4.7 43.6 1.0 CE1 B:HIS63 5.0 52.9 1.0

Iron binding site 3 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:36.6 occ:1.00 FE C:HEM201 0.0 36.6 1.0 ND C:HEM201 1.9 39.9 1.0 NE2 C:HIS87 1.9 58.4 1.0 O1 C:OXY202 2.0 45.3 1.0 NA C:HEM201 2.0 45.7 1.0 NC C:HEM201 2.1 34.4 1.0 NB C:HEM201 2.1 36.2 1.0 O2 C:OXY202 2.8 71.8 1.0 CE1 C:HIS87 2.9 58.1 1.0 C4D C:HEM201 2.9 41.0 1.0 C1D C:HEM201 2.9 36.2 1.0 CD2 C:HIS87 3.0 54.1 1.0 C4B C:HEM201 3.0 37.5 1.0 C1A C:HEM201 3.0 46.5 1.0 C4C C:HEM201 3.1 33.8 1.0 C1B C:HEM201 3.1 38.2 1.0 C1C C:HEM201 3.1 34.0 1.0 C4A C:HEM201 3.1 41.2 1.0 CHA C:HEM201 3.3 48.2 1.0 CHD C:HEM201 3.4 32.9 1.0 CHC C:HEM201 3.4 34.3 1.0 CHB C:HEM201 3.5 39.3 1.0 ND1 C:HIS87 4.0 56.6 1.0 CG C:HIS87 4.1 54.1 1.0 C2D C:HEM201 4.2 35.1 1.0 C3D C:HEM201 4.2 38.7 1.0 C2A C:HEM201 4.3 54.8 1.0 C3A C:HEM201 4.3 48.1 1.0 C2C C:HEM201 4.3 31.4 1.0 C3C C:HEM201 4.3 30.6 1.0 C2B C:HEM201 4.3 42.2 1.0 C3B C:HEM201 4.3 38.9 1.0 NE2 C:HIS58 4.4 71.0 1.0 CE1 C:HIS58 4.6 72.8 1.0 CG2 C:VAL62 4.8 66.7 1.0

Iron binding site 4 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:41.4 occ:1.00 FE D:HEM201 0.0 41.4 1.0 NE2 D:HIS92 1.9 63.1 1.0 ND D:HEM201 1.9 55.9 1.0 O1 D:OXY202 2.0 44.5 1.0 NA D:HEM201 2.0 48.5 1.0 NC D:HEM201 2.1 44.4 1.0 NB D:HEM201 2.1 46.3 1.0 CE1 D:HIS92 2.8 66.6 1.0 C1D D:HEM201 2.9 49.2 1.0 C4D D:HEM201 2.9 53.2 1.0 CD2 D:HIS92 3.0 61.8 1.0 C1A D:HEM201 3.0 52.3 1.0 C4A D:HEM201 3.0 49.2 1.0 O2 D:OXY202 3.1 76.8 1.0 C4C D:HEM201 3.1 44.9 1.0 C1B D:HEM201 3.1 44.3 1.0 C4B D:HEM201 3.1 42.3 1.0 C1C D:HEM201 3.1 44.7 1.0 CHD D:HEM201 3.4 47.0 1.0 CHA D:HEM201 3.4 50.1 1.0 CHB D:HEM201 3.4 45.8 1.0 CHC D:HEM201 3.5 44.6 1.0 ND1 D:HIS92 4.0 66.2 1.0 CG D:HIS92 4.1 63.6 1.0 C2D D:HEM201 4.2 51.6 1.0 C3D D:HEM201 4.2 54.0 1.0 C2A D:HEM201 4.2 54.5 1.0 C3A D:HEM201 4.2 49.7 1.0 C2B D:HEM201 4.3 45.7 1.0 NE2 D:HIS63 4.3 68.9 1.0 C3C D:HEM201 4.3 42.4 1.0 C2C D:HEM201 4.3 41.1 1.0 C3B D:HEM201 4.4 41.3 1.0 CG2 D:VAL67 4.8 68.2 1.0 CE1 D:HIS63 5.0 73.7 1.0

Iron binding site 5 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:69.0 occ:1.00 FE E:HEM201 0.0 69.0 1.0 ND E:HEM201 1.9 54.3 1.0 NA E:HEM201 2.0 74.1 1.0 NB E:HEM201 2.1 56.2 1.0 NE2 E:HIS87 2.1 0.2 1.0 CE1 E:HIS87 2.1 0.8 1.0 NC E:HEM201 2.1 63.2 1.0 C4D E:HEM201 2.9 58.4 1.0 C1D E:HEM201 3.0 52.6 1.0 C1A E:HEM201 3.0 65.0 1.0 C4B E:HEM201 3.0 63.6 1.0 C4A E:HEM201 3.0 78.0 1.0 C1B E:HEM201 3.0 59.2 1.0 C1C E:HEM201 3.1 54.0 1.0 C4C E:HEM201 3.1 63.9 1.0 CHA E:HEM201 3.4 54.2 1.0 CHB E:HEM201 3.4 69.4 1.0 ND1 E:HIS87 3.4 0.4 1.0 CHC E:HEM201 3.4 55.6 1.0 CHD E:HEM201 3.4 66.6 1.0 CD2 E:HIS87 3.5 0.7 1.0 CG E:HIS87 4.1 0.1 1.0 C3A E:HEM201 4.2 79.0 1.0 C2D E:HEM201 4.2 55.3 1.0 C2A E:HEM201 4.2 79.7 1.0 C3D E:HEM201 4.2 60.9 1.0 C2B E:HEM201 4.3 62.3 1.0 C2C E:HEM201 4.3 63.1 1.0 C3B E:HEM201 4.3 60.5 1.0 C3C E:HEM201 4.4 55.9 1.0 NE2 E:HIS58 4.4 0.1 1.0 CE1 E:HIS58 4.6 0.5 1.0 CG2 E:VAL62 4.7 0.2 1.0

Iron binding site 6 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe201 b:34.0 occ:1.00 FE F:HEM201 0.0 34.0 1.0 O1 F:OXY202 1.9 78.8 1.0 ND F:HEM201 1.9 36.9 1.0 NA F:HEM201 2.0 34.0 1.0 NE2 F:HIS92 2.0 39.6 1.0 NC F:HEM201 2.0 31.2 1.0 NB F:HEM201 2.1 33.6 1.0 O2 F:OXY202 2.7 81.6 1.0 C1D F:HEM201 2.9 36.0 1.0 C4D F:HEM201 2.9 35.2 1.0 CE1 F:HIS92 3.0 38.3 1.0 C1A F:HEM201 3.0 35.6 1.0 C4C F:HEM201 3.0 34.5 1.0 C4A F:HEM201 3.0 35.5 1.0 CD2 F:HIS92 3.0 33.9 1.0 C4B F:HEM201 3.0 30.1 1.0 C1C F:HEM201 3.0 31.6 1.0 C1B F:HEM201 3.1 33.3 1.0 CHD F:HEM201 3.4 40.4 1.0 CHA F:HEM201 3.4 32.6 1.0 CHC F:HEM201 3.4 29.8 1.0 CHB F:HEM201 3.4 34.1 1.0 ND1 F:HIS92 4.1 35.3 1.0 CG F:HIS92 4.2 33.7 1.0 C2D F:HEM201 4.2 36.8 1.0 C3A F:HEM201 4.2 35.8 1.0 C2A F:HEM201 4.2 41.5 1.0 C3D F:HEM201 4.2 41.5 1.0 C2C F:HEM201 4.2 31.3 1.0 C3C F:HEM201 4.2 34.1 1.0 C2B F:HEM201 4.3 29.7 1.0 NE2 F:HIS63 4.3 92.4 1.0 C3B F:HEM201 4.3 32.1 1.0 CG2 F:VAL67 4.6 72.6 1.0 CE1 F:HIS63 4.9 96.7 1.0

Iron binding site 7 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe201 b:48.3 occ:1.00 FE G:HEM201 0.0 48.3 1.0 ND G:HEM201 1.9 37.1 1.0 NE2 G:HIS87 1.9 99.0 1.0 NA G:HEM201 2.0 54.5 1.0 NB G:HEM201 2.0 42.6 1.0 NC G:HEM201 2.1 43.4 1.0 O2 G:OXY202 2.4 80.9 1.0 C1D G:HEM201 2.9 44.9 1.0 CE1 G:HIS87 2.9 0.7 1.0 C4D G:HEM201 2.9 47.8 1.0 CD2 G:HIS87 3.0 95.8 1.0 O1 G:OXY202 3.0 0.7 1.0 C4B G:HEM201 3.0 48.0 1.0 C1A G:HEM201 3.0 51.1 1.0 C1B G:HEM201 3.0 55.6 1.0 C4A G:HEM201 3.1 50.8 1.0 C4C G:HEM201 3.1 35.9 1.0 C1C G:HEM201 3.2 42.0 1.0 CHD G:HEM201 3.4 40.7 1.0 CHA G:HEM201 3.4 46.8 1.0 CHB G:HEM201 3.5 50.2 1.0 CHC G:HEM201 3.5 42.7 1.0 ND1 G:HIS87 4.0 0.7 1.0 CG G:HIS87 4.1 0.4 1.0 C2D G:HEM201 4.2 37.8 1.0 C3D G:HEM201 4.2 43.8 1.0 C2A G:HEM201 4.2 64.5 1.0 C3A G:HEM201 4.2 61.7 1.0 C2B G:HEM201 4.3 51.9 1.0 C3B G:HEM201 4.3 47.2 1.0 C3C G:HEM201 4.3 40.1 1.0 C2C G:HEM201 4.4 43.9 1.0 NE2 G:HIS58 4.4 82.9 1.0 CE1 G:HIS58 4.7 88.1 1.0 CG2 G:VAL62 4.9 78.7 1.0

Iron binding site 8 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe201 b:75.3 occ:1.00 FE H:HEM201 0.0 75.3 1.0 ND H:HEM201 1.9 73.7 1.0 NE2 H:HIS92 2.0 0.1 1.0 NA H:HEM201 2.0 70.6 1.0 NC H:HEM201 2.1 61.9 1.0 NB H:HEM201 2.1 75.3 1.0 CE1 H:HIS92 2.8 1.0 1.0 C4D H:HEM201 2.9 70.1 1.0 C1D H:HEM201 2.9 72.6 1.0 C1A H:HEM201 3.0 77.2 1.0 C1C H:HEM201 3.0 55.7 1.0 C4B H:HEM201 3.0 61.6 1.0 C4A H:HEM201 3.1 77.6 1.0 C1B H:HEM201 3.1 78.3 1.0 C4C H:HEM201 3.1 52.7 1.0 CD2 H:HIS92 3.1 0.6 1.0 CHA H:HEM201 3.3 70.0 1.0 CHC H:HEM201 3.4 54.5 1.0 CHD H:HEM201 3.4 59.8 1.0 CHB H:HEM201 3.5 81.4 1.0 ND1 H:HIS92 4.0 0.6 1.0 CG H:HIS92 4.2 0.1 1.0 C3D H:HEM201 4.2 86.8 1.0 C2D H:HEM201 4.2 78.1 1.0 C2A H:HEM201 4.2 83.1 1.0 C2C H:HEM201 4.2 60.6 1.0 C3A H:HEM201 4.2 77.0 1.0 NE2 H:HIS63 4.2 0.0 1.0 C3C H:HEM201 4.3 53.1 1.0 C2B H:HEM201 4.3 68.1 1.0 C3B H:HEM201 4.3 63.1 1.0 CG2 H:VAL67 4.5 0.1 1.0 CE1 H:HIS63 4.9 0.1 1.0

Iron binding site 9 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ S:Fe201 b:50.7 occ:1.00 FE S:HEM201 0.0 50.7 1.0 ND S:HEM201 1.9 45.7 1.0 NE2 S:HIS87 1.9 93.8 1.0 NA S:HEM201 2.0 50.8 1.0 O1 S:OXY202 2.0 63.8 1.0 NB S:HEM201 2.1 44.3 1.0 NC S:HEM201 2.1 44.1 1.0 CE1 S:HIS87 2.8 95.0 1.0 C4D S:HEM201 2.9 42.9 1.0 C1D S:HEM201 2.9 51.0 1.0 C4B S:HEM201 3.0 41.5 1.0 C1A S:HEM201 3.0 45.6 1.0 C4A S:HEM201 3.0 52.6 1.0 C1C S:HEM201 3.0 40.5 1.0 CD2 S:HIS87 3.0 89.2 1.0 C1B S:HEM201 3.1 48.3 1.0 C4C S:HEM201 3.1 45.1 1.0 O2 S:OXY202 3.1 88.6 1.0 CHA S:HEM201 3.3 41.4 1.0 CHC S:HEM201 3.4 40.5 1.0 CHD S:HEM201 3.4 45.4 1.0 CHB S:HEM201 3.5 53.0 1.0 ND1 S:HIS87 4.0 94.6 1.0 CG S:HIS87 4.1 89.9 1.0 C3D S:HEM201 4.1 46.2 1.0 C2D S:HEM201 4.2 41.7 1.0 C2A S:HEM201 4.2 54.5 1.0 C3A S:HEM201 4.2 54.2 1.0 C2C S:HEM201 4.2 44.1 1.0 C3B S:HEM201 4.2 41.0 1.0 C2B S:HEM201 4.3 38.9 1.0 C3C S:HEM201 4.3 37.9 1.0 NE2 S:HIS58 4.5 0.1 1.0 CE1 S:HIS58 4.5 0.6 1.0 CG2 S:VAL62 4.8 99.9 1.0

Iron binding site 10 out of 10 in the Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes within 5.0Å range: probe atom residue distance (Å) B Occ T:Fe201 b:71.2 occ:1.00 FE T:HEM201 0.0 71.2 1.0 NE2 T:HIS92 1.9 0.8 1.0 ND T:HEM201 1.9 0.4 1.0 O1 T:OXY202 2.0 56.6 1.0 NA T:HEM201 2.0 0.6 1.0 NB T:HEM201 2.1 97.7 1.0 NC T:HEM201 2.1 96.3 1.0 CE1 T:HIS92 2.8 0.7 1.0 C4D T:HEM201 2.9 0.2 1.0 C1D T:HEM201 3.0 99.3 1.0 CD2 T:HIS92 3.0 0.1 1.0 C1A T:HEM201 3.0 0.9 1.0 C4A T:HEM201 3.1 0.9 1.0 O2 T:OXY202 3.1 84.8 1.0 C1B T:HEM201 3.1 98.7 1.0 C4B T:HEM201 3.1 90.0 1.0 C4C T:HEM201 3.1 91.0 1.0 C1C T:HEM201 3.1 82.7 1.0 CHA T:HEM201 3.4 0.1 1.0 CHD T:HEM201 3.4 96.1 1.0 CHB T:HEM201 3.5 0.4 1.0 CHC T:HEM201 3.5 83.3 1.0 ND1 T:HIS92 4.0 0.9 1.0 CG T:HIS92 4.1 0.8 1.0 C3D T:HEM201 4.2 1.0 1.0 C2D T:HEM201 4.2 0.7 1.0 C2A T:HEM201 4.2 0.3 1.0 NE2 T:HIS63 4.2 0.8 1.0 C3A T:HEM201 4.2 0.8 1.0 C2B T:HEM201 4.3 91.9 1.0 C2C T:HEM201 4.3 89.6 1.0 C3C T:HEM201 4.3 85.3 1.0 C3B T:HEM201 4.4 92.5 1.0 CG1 T:VAL67 4.5 0.2 1.0 CE1 T:HIS63 4.9 0.5 1.0

N.T.Saraswathi, N.S.Pannu, V.E.Syakhovich, A.Saurabh, S.B.Bokut, D.Moras, M.Ruff. Glycation Restrains Allosteric Transition in Hemoglobin: the Molecular Basis of Oxidative Stress Under Hyperglycemic Conditions in Diabetes To Be Published.