Iron in PDB 1yhr: T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets)

The structure of T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets), PDB code: 1yhr was solved by J.S.Kavanaugh, P.H.Rogers, A.Arnone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.200, 98.400, 66.500, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 27

The binding sites of Iron atom in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets) (pdb code 1yhr). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets), PDB code: 1yhr:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:13.7 occ:1.00 FE A:HEM142 0.0 13.7 1.0 O1 A:OXY150 1.7 20.9 1.0 NA A:HEM142 1.9 16.1 1.0 NB A:HEM142 2.0 14.5 1.0 ND A:HEM142 2.0 14.1 1.0 O2 A:OXY150 2.0 21.9 1.0 NC A:HEM142 2.1 12.6 1.0 NE2 A:HIS87 2.1 28.3 1.0 C4A A:HEM142 2.9 16.0 1.0 C1A A:HEM142 2.9 17.6 1.0 C1B A:HEM142 3.0 15.1 1.0 C4D A:HEM142 3.0 17.4 1.0 CE1 A:HIS87 3.0 33.0 1.0 C1D A:HEM142 3.0 14.7 1.0 C4C A:HEM142 3.0 11.3 1.0 CD2 A:HIS87 3.1 33.1 1.0 C4B A:HEM142 3.1 14.0 1.0 C1C A:HEM142 3.1 10.2 1.0 CHB A:HEM142 3.3 15.3 1.0 CHA A:HEM142 3.3 18.1 1.0 CHD A:HEM142 3.4 14.7 1.0 CHC A:HEM142 3.5 12.2 1.0 ND1 A:HIS87 4.1 33.5 1.0 C3A A:HEM142 4.1 17.6 1.0 C2A A:HEM142 4.2 20.1 1.0 CG A:HIS87 4.2 35.0 1.0 C2B A:HEM142 4.2 14.1 1.0 C3B A:HEM142 4.2 14.4 1.0 C3C A:HEM142 4.2 8.5 1.0 C3D A:HEM142 4.3 19.4 1.0 C2D A:HEM142 4.3 17.0 1.0 C2C A:HEM142 4.3 8.5 1.0 NE2 A:HIS58 4.4 23.4 1.0 CE1 A:HIS58 4.6 22.9 1.0

Iron binding site 2 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:6.6 occ:1.00 FE B:HEM147 0.0 6.6 1.0 O1 B:OXY150 1.7 2.5 1.0 NC B:HEM147 1.9 4.6 1.0 NB B:HEM147 2.1 2.0 1.0 NE2 B:HIS92 2.1 6.3 1.0 NA B:HEM147 2.1 2.7 1.0 ND B:HEM147 2.1 2.0 1.0 O2 B:OXY150 2.4 6.9 1.0 CD2 B:HIS92 2.8 2.2 1.0 C1C B:HEM147 2.9 5.6 1.0 C4B B:HEM147 2.9 2.5 1.0 C4C B:HEM147 2.9 5.3 1.0 C1D B:HEM147 3.0 3.3 1.0 C1B B:HEM147 3.1 3.7 1.0 C1A B:HEM147 3.1 5.5 1.0 C4A B:HEM147 3.1 5.2 1.0 CE1 B:HIS92 3.2 7.8 1.0 C4D B:HEM147 3.2 6.5 1.0 CHC B:HEM147 3.3 5.7 1.0 CHD B:HEM147 3.3 6.1 1.0 CHB B:HEM147 3.5 4.8 1.0 CHA B:HEM147 3.6 6.2 1.0 CG B:HIS92 4.0 6.7 1.0 C2C B:HEM147 4.1 5.5 1.0 C3C B:HEM147 4.1 2.8 1.0 C3B B:HEM147 4.2 5.5 1.0 ND1 B:HIS92 4.2 8.4 1.0 C2B B:HEM147 4.3 2.6 1.0 C3A B:HEM147 4.3 3.8 1.0 C2A B:HEM147 4.4 2.0 1.0 C2D B:HEM147 4.4 6.0 1.0 C3D B:HEM147 4.4 2.4 1.0 NE2 B:HIS63 4.6 6.1 1.0

Iron binding site 3 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:19.1 occ:1.00 FE C:HEM142 0.0 19.1 1.0 O1 C:OXY150 1.7 17.2 1.0 NB C:HEM142 1.9 19.1 1.0 NA C:HEM142 2.0 22.7 1.0 NC C:HEM142 2.0 17.7 1.0 ND C:HEM142 2.1 19.4 1.0 NE2 C:HIS87 2.1 36.2 1.0 O2 C:OXY150 2.8 16.9 1.0 CE1 C:HIS87 2.8 40.4 1.0 C4B C:HEM142 2.9 19.1 1.0 C1C C:HEM142 2.9 15.8 1.0 C1B C:HEM142 3.0 20.3 1.0 C4A C:HEM142 3.0 24.4 1.0 C1A C:HEM142 3.0 24.3 1.0 C4D C:HEM142 3.0 22.6 1.0 C4C C:HEM142 3.1 15.5 1.0 C1D C:HEM142 3.1 18.5 1.0 CD2 C:HIS87 3.2 43.2 1.0 CHC C:HEM142 3.3 17.6 1.0 CHB C:HEM142 3.4 24.1 1.0 CHA C:HEM142 3.4 23.6 1.0 CHD C:HEM142 3.5 17.9 1.0 ND1 C:HIS87 4.0 42.9 1.0 C3B C:HEM142 4.1 17.3 1.0 C2B C:HEM142 4.2 19.7 1.0 C2C C:HEM142 4.2 17.7 1.0 C3A C:HEM142 4.2 26.9 1.0 C3C C:HEM142 4.2 15.1 1.0 C2A C:HEM142 4.2 27.5 1.0 CG C:HIS87 4.3 48.2 1.0 C3D C:HEM142 4.3 20.7 1.0 C2D C:HEM142 4.3 19.3 1.0 NE2 C:HIS58 4.6 17.6 1.0 CE1 C:HIS58 4.6 17.4 1.0 CG2 C:VAL62 5.0 19.8 1.0

Iron binding site 4 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of T-to-T(High) Quaternary Transitions in Human Hemoglobin: Hba Oxy (10.0MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:20.8 occ:1.00 FE D:HEM147 0.0 20.8 1.0 O1 D:OXY150 1.7 15.4 1.0 NC D:HEM147 1.8 18.4 1.0 NB D:HEM147 2.0 22.9 1.0 NE2 D:HIS92 2.1 13.5 1.0 ND D:HEM147 2.1 21.6 1.0 NA D:HEM147 2.2 24.8 1.0 O2 D:OXY150 2.7 15.4 1.0 C4C D:HEM147 2.7 18.2 1.0 C1C D:HEM147 2.8 17.5 1.0 C4B D:HEM147 2.9 23.2 1.0 CD2 D:HIS92 2.9 12.7 1.0 C1D D:HEM147 2.9 23.5 1.0 C1B D:HEM147 3.0 24.4 1.0 C4A D:HEM147 3.1 25.3 1.0 CE1 D:HIS92 3.1 12.0 1.0 CHD D:HEM147 3.2 20.8 1.0 CHC D:HEM147 3.2 21.3 1.0 C4D D:HEM147 3.3 25.6 1.0 C1A D:HEM147 3.3 27.9 1.0 CHB D:HEM147 3.5 25.1 1.0 CHA D:HEM147 3.7 27.9 1.0 C3C D:HEM147 3.9 17.5 1.0 C2C D:HEM147 4.0 17.1 1.0 CG D:HIS92 4.1 16.9 1.0 C3B D:HEM147 4.1 23.1 1.0 ND1 D:HIS92 4.2 13.7 1.0 C2B D:HEM147 4.2 24.1 1.0 C2D D:HEM147 4.3 24.5 1.0 C3A D:HEM147 4.4 27.9 1.0 C3D D:HEM147 4.4 27.3 1.0 C2A D:HEM147 4.5 29.4 1.0 NE2 D:HIS63 4.6 19.6 1.0 CE1 D:HIS63 4.9 20.6 1.0

J.S.Kavanaugh, P.H.Rogers, A.Arnone. Crystallographic Evidence For A New Ensemble of Ligand-Induced Allosteric Transitions in Hemoglobin: the T-to-T(High) Quaternary Transitions. Biochemistry V. 44 6101 2005.
ISSN: ISSN 0006-2960
PubMed: 15835899
DOI: 10.1021/BI047813A