Iron in PDB 1ygf: T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set)

The structure of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set), PDB code: 1ygf 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 (°)	96.500, 98.300, 66.100, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 27

The binding sites of Iron atom in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set) (pdb code 1ygf). 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: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set), PDB code: 1ygf:
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: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set)


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: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:31.4 occ:1.00 FE A:HEM142 0.0 31.4 1.0 O1 A:OXY150 1.7 30.2 1.0 NA A:HEM142 2.0 30.5 1.0 ND A:HEM142 2.0 31.3 1.0 NB A:HEM142 2.0 29.2 1.0 NC A:HEM142 2.1 30.4 1.0 NE2 A:HIS87 2.2 30.6 1.0 O2 A:OXY150 2.5 30.8 1.0 C4D A:HEM142 3.0 34.6 1.0 C1A A:HEM142 3.0 32.3 1.0 CE1 A:HIS87 3.0 31.9 1.0 C1B A:HEM142 3.0 27.4 1.0 C4B A:HEM142 3.1 27.5 1.0 C4A A:HEM142 3.1 28.9 1.0 C1C A:HEM142 3.1 30.6 1.0 C1D A:HEM142 3.1 31.6 1.0 C4C A:HEM142 3.1 30.0 1.0 CHA A:HEM142 3.3 34.2 1.0 CD2 A:HIS87 3.4 33.2 1.0 CHB A:HEM142 3.4 27.6 1.0 CHC A:HEM142 3.5 29.0 1.0 CHD A:HEM142 3.5 29.5 1.0 ND1 A:HIS87 4.2 32.4 1.0 C2A A:HEM142 4.2 33.1 1.0 C3D A:HEM142 4.2 35.9 1.0 C3A A:HEM142 4.3 32.9 1.0 C3B A:HEM142 4.3 26.8 1.0 C2B A:HEM142 4.3 26.2 1.0 C2D A:HEM142 4.3 35.6 1.0 C3C A:HEM142 4.3 29.8 1.0 C2C A:HEM142 4.4 29.6 1.0 CG A:HIS87 4.4 36.0 1.0 NE2 A:HIS58 4.7 34.2 1.0 CE1 A:HIS58 4.8 35.7 1.0 CG2 A:VAL62 5.0 31.6 1.0 CD1 A:LEU91 5.0 47.6 1.0

Iron binding site 2 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set)


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: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:22.6 occ:1.00 FE B:HEM147 0.0 22.6 1.0 O1 B:OXY150 1.8 23.4 1.0 NE2 B:HIS92 1.9 21.3 1.0 NC B:HEM147 2.0 21.1 1.0 NA B:HEM147 2.0 20.5 1.0 NB B:HEM147 2.0 21.7 1.0 ND B:HEM147 2.1 21.8 1.0 CE1 B:HIS92 2.8 20.6 1.0 O2 B:OXY150 2.8 29.2 1.0 C4A B:HEM147 2.9 19.0 1.0 C4C B:HEM147 2.9 21.2 1.0 C1B B:HEM147 2.9 22.3 1.0 C1D B:HEM147 3.0 24.0 1.0 CD2 B:HIS92 3.0 20.0 1.0 C1C B:HEM147 3.0 22.1 1.0 C4B B:HEM147 3.0 23.4 1.0 C1A B:HEM147 3.1 21.1 1.0 CHB B:HEM147 3.2 20.7 1.0 CHD B:HEM147 3.2 23.3 1.0 C4D B:HEM147 3.3 22.9 1.0 CHC B:HEM147 3.4 23.7 1.0 CHA B:HEM147 3.6 22.6 1.0 ND1 B:HIS92 3.9 19.7 1.0 CG B:HIS92 4.1 19.2 1.0 C3A B:HEM147 4.1 19.9 1.0 C3C B:HEM147 4.1 22.1 1.0 C2B B:HEM147 4.2 24.0 1.0 C2C B:HEM147 4.2 21.6 1.0 C3B B:HEM147 4.2 24.8 1.0 C2A B:HEM147 4.3 19.8 1.0 C2D B:HEM147 4.3 25.0 1.0 C3D B:HEM147 4.5 25.0 1.0 CG2 B:VAL67 4.7 27.3 1.0 NE2 B:HIS63 4.8 26.1 1.0

Iron binding site 3 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set)


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: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:36.0 occ:1.00 FE C:HEM142 0.0 36.0 1.0 O1 C:OXY150 1.7 37.9 1.0 NB C:HEM142 2.0 35.6 1.0 NA C:HEM142 2.0 38.5 1.0 NC C:HEM142 2.1 36.1 1.0 ND C:HEM142 2.1 35.2 1.0 NE2 C:HIS87 2.4 38.6 1.0 O2 C:OXY150 2.5 40.6 1.0 C4B C:HEM142 3.0 35.7 1.0 C1B C:HEM142 3.0 35.5 1.0 C1A C:HEM142 3.0 37.6 1.0 C1C C:HEM142 3.0 34.3 1.0 C4A C:HEM142 3.0 38.3 1.0 C4D C:HEM142 3.1 33.7 1.0 C1D C:HEM142 3.1 34.0 1.0 C4C C:HEM142 3.1 34.3 1.0 CE1 C:HIS87 3.2 40.0 1.0 CHC C:HEM142 3.3 35.5 1.0 CHA C:HEM142 3.4 35.0 1.0 CHB C:HEM142 3.4 37.1 1.0 CHD C:HEM142 3.5 34.6 1.0 CD2 C:HIS87 3.5 41.3 1.0 C3B C:HEM142 4.2 35.3 1.0 C2B C:HEM142 4.2 34.2 1.0 C2A C:HEM142 4.2 39.3 1.0 C3A C:HEM142 4.2 39.5 1.0 C2C C:HEM142 4.3 33.5 1.0 C3C C:HEM142 4.3 34.3 1.0 C3D C:HEM142 4.3 34.0 1.0 C2D C:HEM142 4.3 31.7 1.0 NE2 C:HIS58 4.3 41.5 1.0 ND1 C:HIS87 4.4 42.3 1.0 CE1 C:HIS58 4.5 42.7 1.0 CG C:HIS87 4.6 45.8 1.0 CG2 C:VAL62 4.9 44.6 1.0

Iron binding site 4 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set)


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: BETAH97A Oxy (2MM Ihp, 20% Peg) (1 Test Set) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:36.7 occ:1.00 FE D:HEM147 0.0 36.7 1.0 O1 D:OXY150 1.8 38.5 1.0 NE2 D:HIS92 2.0 37.3 1.0 NA D:HEM147 2.0 39.0 1.0 NB D:HEM147 2.0 37.4 1.0 NC D:HEM147 2.0 38.1 1.0 ND D:HEM147 2.1 38.1 1.0 O2 D:OXY150 2.7 42.2 1.0 CE1 D:HIS92 2.9 35.4 1.0 C1B D:HEM147 3.0 38.4 1.0 C4A D:HEM147 3.0 39.6 1.0 C4C D:HEM147 3.1 38.3 1.0 C1D D:HEM147 3.1 38.8 1.0 C4D D:HEM147 3.1 39.3 1.0 C1C D:HEM147 3.1 37.8 1.0 C1A D:HEM147 3.1 41.5 1.0 CD2 D:HIS92 3.1 36.2 1.0 C4B D:HEM147 3.1 37.6 1.0 CHB D:HEM147 3.3 39.1 1.0 CHD D:HEM147 3.4 38.8 1.0 CHA D:HEM147 3.4 40.7 1.0 CHC D:HEM147 3.5 38.6 1.0 ND1 D:HIS92 4.0 34.0 1.0 CG D:HIS92 4.2 34.0 1.0 C2B D:HEM147 4.2 40.0 1.0 C3C D:HEM147 4.3 37.5 1.0 C3A D:HEM147 4.3 41.8 1.0 C2C D:HEM147 4.3 37.3 1.0 C2D D:HEM147 4.3 39.7 1.0 NE2 D:HIS63 4.3 43.4 1.0 C3B D:HEM147 4.3 39.7 1.0 C3D D:HEM147 4.3 39.6 1.0 C2A D:HEM147 4.3 43.4 1.0 CG2 D:VAL67 4.5 47.2 1.0 CE1 D:HIS63 4.9 44.8 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