Iron in PDB 1yg5: T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets)

The structure of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets), PDB code: 1yg5 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 / 2.70
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.570, 98.590, 66.770, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 27.3

The binding sites of Iron atom in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets) (pdb code 1yg5). 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: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets), PDB code: 1yg5:
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: BETAW37H Oxy (2MM 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: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:29.9 occ:1.00 FE A:HEM142 0.0 29.9 1.0 O1 A:OXY150 1.7 32.1 1.0 ND A:HEM142 1.9 29.1 1.0 NA A:HEM142 1.9 30.6 1.0 NC A:HEM142 1.9 26.6 1.0 NE2 A:HIS87 2.0 30.8 1.0 NB A:HEM142 2.1 27.8 1.0 O2 A:OXY150 2.7 36.6 1.0 C4D A:HEM142 2.9 31.0 1.0 C1A A:HEM142 2.9 32.2 1.0 CE1 A:HIS87 2.9 34.4 1.0 C4C A:HEM142 3.0 25.8 1.0 C1D A:HEM142 3.0 29.1 1.0 C1C A:HEM142 3.0 25.6 1.0 CD2 A:HIS87 3.0 33.3 1.0 C4A A:HEM142 3.0 32.7 1.0 C4B A:HEM142 3.1 26.6 1.0 C1B A:HEM142 3.1 25.6 1.0 CHA A:HEM142 3.2 33.7 1.0 CHD A:HEM142 3.3 28.2 1.0 CHB A:HEM142 3.4 30.1 1.0 CHC A:HEM142 3.5 25.2 1.0 ND1 A:HIS87 4.1 34.2 1.0 CG A:HIS87 4.1 33.1 1.0 C2C A:HEM142 4.2 22.3 1.0 C3D A:HEM142 4.2 31.5 1.0 C3C A:HEM142 4.2 23.8 1.0 C2A A:HEM142 4.2 34.8 1.0 C2D A:HEM142 4.2 30.7 1.0 C3A A:HEM142 4.2 32.0 1.0 C3B A:HEM142 4.3 25.7 1.0 C2B A:HEM142 4.3 24.8 1.0 NE2 A:HIS58 4.6 34.8 1.0 CE1 A:HIS58 4.8 33.6 1.0 CD1 A:LEU91 4.8 39.6 1.0

Iron binding site 2 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAW37H Oxy (2MM 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: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:17.8 occ:1.00 FE B:HEM147 0.0 17.8 1.0 NA B:HEM147 1.7 11.6 1.0 O1 B:OXY150 1.8 18.2 1.0 NC B:HEM147 1.8 13.0 1.0 NB B:HEM147 2.0 15.8 1.0 NE2 B:HIS92 2.0 23.1 1.0 ND B:HEM147 2.2 15.1 1.0 CE1 B:HIS92 2.4 18.7 1.0 O2 B:OXY150 2.8 23.6 1.0 C4A B:HEM147 2.8 11.7 1.0 C1A B:HEM147 2.8 8.7 1.0 C1C B:HEM147 2.8 9.7 1.0 C4C B:HEM147 2.9 12.2 1.0 C4B B:HEM147 3.0 16.0 1.0 C1B B:HEM147 3.0 14.0 1.0 C1D B:HEM147 3.2 19.1 1.0 CD2 B:HIS92 3.2 20.6 1.0 C4D B:HEM147 3.3 16.1 1.0 CHC B:HEM147 3.3 12.8 1.0 CHB B:HEM147 3.3 12.0 1.0 CHD B:HEM147 3.4 16.7 1.0 CHA B:HEM147 3.5 8.7 1.0 ND1 B:HIS92 3.6 19.6 1.0 C3C B:HEM147 4.0 5.7 1.0 C3A B:HEM147 4.0 4.2 1.0 C2C B:HEM147 4.0 7.1 1.0 C2A B:HEM147 4.0 9.1 1.0 CG B:HIS92 4.0 20.4 1.0 C3B B:HEM147 4.2 15.4 1.0 C2B B:HEM147 4.2 14.5 1.0 C2D B:HEM147 4.5 20.4 1.0 C3D B:HEM147 4.5 20.8 1.0 NE2 B:HIS63 4.6 22.1 1.0 CG2 B:VAL67 4.8 21.8 1.0

Iron binding site 3 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAW37H Oxy (2MM 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: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:27.3 occ:1.00 FE C:HEM142 0.0 27.3 1.0 O1 C:OXY150 1.7 27.9 1.0 NC C:HEM142 1.9 27.3 1.0 NA C:HEM142 1.9 30.3 1.0 NB C:HEM142 1.9 31.4 1.0 NE2 C:HIS87 2.0 35.6 1.0 ND C:HEM142 2.1 27.4 1.0 CE1 C:HIS87 2.3 36.0 1.0 O2 C:OXY150 2.7 32.2 1.0 C4A C:HEM142 2.9 30.6 1.0 C1C C:HEM142 2.9 26.1 1.0 C4C C:HEM142 2.9 26.0 1.0 C1B C:HEM142 3.0 30.4 1.0 C4B C:HEM142 3.0 30.9 1.0 C1A C:HEM142 3.0 31.2 1.0 C4D C:HEM142 3.1 27.1 1.0 C1D C:HEM142 3.1 23.6 1.0 CHB C:HEM142 3.3 30.2 1.0 CHC C:HEM142 3.3 28.4 1.0 CD2 C:HIS87 3.4 40.6 1.0 CHD C:HEM142 3.4 25.1 1.0 CHA C:HEM142 3.4 27.1 1.0 ND1 C:HIS87 3.6 38.8 1.0 C2C C:HEM142 4.1 25.4 1.0 C3C C:HEM142 4.1 24.7 1.0 CG C:HIS87 4.1 43.0 1.0 C3A C:HEM142 4.1 33.7 1.0 C2B C:HEM142 4.2 31.9 1.0 C3B C:HEM142 4.2 31.7 1.0 C2A C:HEM142 4.2 33.0 1.0 C3D C:HEM142 4.3 25.1 1.0 C2D C:HEM142 4.4 24.3 1.0 NE2 C:HIS58 4.6 30.6 1.0 CG2 C:VAL62 4.7 26.8 1.0

Iron binding site 4 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAW37H Oxy (2MM 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: BETAW37H Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:32.1 occ:1.00 FE D:HEM147 0.0 32.1 1.0 O1 D:OXY150 1.8 25.1 1.0 NA D:HEM147 2.0 31.2 1.0 NE2 D:HIS92 2.0 28.9 1.0 NC D:HEM147 2.0 27.0 1.0 ND D:HEM147 2.0 28.9 1.0 NB D:HEM147 2.0 30.4 1.0 CE1 D:HIS92 2.6 31.9 1.0 O2 D:OXY150 2.9 31.5 1.0 C4A D:HEM147 2.9 32.2 1.0 C1C D:HEM147 2.9 25.4 1.0 C4B D:HEM147 3.0 30.9 1.0 C1D D:HEM147 3.0 30.6 1.0 C4C D:HEM147 3.0 24.4 1.0 C1B D:HEM147 3.1 29.4 1.0 C4D D:HEM147 3.1 29.6 1.0 C1A D:HEM147 3.1 31.6 1.0 CD2 D:HIS92 3.2 32.0 1.0 CHC D:HEM147 3.3 29.0 1.0 CHB D:HEM147 3.3 31.1 1.0 CHD D:HEM147 3.4 27.4 1.0 CHA D:HEM147 3.5 31.0 1.0 ND1 D:HIS92 3.8 32.4 1.0 C2C D:HEM147 4.2 24.5 1.0 CG D:HIS92 4.2 31.8 1.0 C3C D:HEM147 4.2 25.2 1.0 C3A D:HEM147 4.2 31.2 1.0 C3B D:HEM147 4.2 30.6 1.0 C2D D:HEM147 4.2 30.4 1.0 C2B D:HEM147 4.2 29.0 1.0 C3D D:HEM147 4.3 31.2 1.0 C2A D:HEM147 4.3 33.6 1.0 NE2 D:HIS63 4.5 32.2 1.0 CE1 D:HIS63 4.9 33.6 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