Iron in PDB 1yen: T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets)

The structure of T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets), PDB code: 1yen 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 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.500, 98.400, 67.200, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 26.7

The binding sites of Iron atom in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets) (pdb code 1yen). 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: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets), PDB code: 1yen:
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: BETAP36A 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: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:41.2 occ:1.00 FE A:HEM142 0.0 41.2 1.0 O1 A:OXY150 1.8 47.8 1.0 NA A:HEM142 1.9 43.2 1.0 NC A:HEM142 1.9 41.4 1.0 ND A:HEM142 1.9 44.9 1.0 NB A:HEM142 2.1 42.6 1.0 NE2 A:HIS87 2.1 50.7 1.0 O2 A:OXY150 2.8 47.7 1.0 C1A A:HEM142 2.9 47.3 1.0 C4A A:HEM142 2.9 44.1 1.0 C4D A:HEM142 3.0 47.8 1.0 C4C A:HEM142 3.0 40.9 1.0 C1D A:HEM142 3.0 45.5 1.0 C1C A:HEM142 3.0 42.1 1.0 CD2 A:HIS87 3.0 54.2 1.0 CE1 A:HIS87 3.1 51.2 1.0 C1B A:HEM142 3.1 42.9 1.0 C4B A:HEM142 3.1 43.3 1.0 CHA A:HEM142 3.3 48.2 1.0 CHD A:HEM142 3.3 44.1 1.0 CHB A:HEM142 3.4 44.2 1.0 CHC A:HEM142 3.5 43.3 1.0 C2A A:HEM142 4.1 49.2 1.0 C3A A:HEM142 4.1 45.8 1.0 ND1 A:HIS87 4.2 53.2 1.0 C3C A:HEM142 4.2 39.1 1.0 CG A:HIS87 4.2 55.8 1.0 C3D A:HEM142 4.2 50.8 1.0 C2C A:HEM142 4.2 40.5 1.0 C2D A:HEM142 4.2 48.4 1.0 C2B A:HEM142 4.3 41.7 1.0 C3B A:HEM142 4.4 42.5 1.0 NE2 A:HIS58 4.6 52.5 1.0 CE1 A:HIS58 4.6 52.9 1.0

Iron binding site 2 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAP36A 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: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:32.5 occ:1.00 FE B:HEM147 0.0 32.5 1.0 O1 B:OXY150 1.8 31.8 1.0 NA B:HEM147 1.9 32.0 1.0 NC B:HEM147 1.9 35.0 1.0 NB B:HEM147 2.1 33.4 1.0 NE2 B:HIS92 2.1 34.4 1.0 ND B:HEM147 2.1 32.8 1.0 O2 B:OXY150 2.8 39.9 1.0 C4C B:HEM147 2.9 33.0 1.0 C4A B:HEM147 2.9 31.5 1.0 C1A B:HEM147 3.0 30.9 1.0 C1D B:HEM147 3.0 33.7 1.0 C1B B:HEM147 3.0 32.4 1.0 C1C B:HEM147 3.1 35.7 1.0 CD2 B:HIS92 3.1 34.8 1.0 C4B B:HEM147 3.1 36.5 1.0 CE1 B:HIS92 3.1 32.1 1.0 CHD B:HEM147 3.2 35.1 1.0 C4D B:HEM147 3.2 34.2 1.0 CHB B:HEM147 3.3 32.2 1.0 CHC B:HEM147 3.5 37.8 1.0 CHA B:HEM147 3.5 32.6 1.0 C3C B:HEM147 4.1 31.4 1.0 C3A B:HEM147 4.1 29.1 1.0 C2A B:HEM147 4.1 30.9 1.0 C2C B:HEM147 4.2 34.3 1.0 ND1 B:HIS92 4.2 31.1 1.0 CG B:HIS92 4.2 33.0 1.0 C2B B:HEM147 4.2 36.9 1.0 C3B B:HEM147 4.3 36.0 1.0 C2D B:HEM147 4.3 35.5 1.0 C3D B:HEM147 4.4 35.7 1.0 NE2 B:HIS63 4.7 38.0 1.0 CG2 B:VAL67 4.8 38.2 1.0

Iron binding site 3 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAP36A 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: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:46.9 occ:1.00 FE C:HEM142 0.0 46.9 1.0 O1 C:OXY150 1.7 45.9 1.0 NC C:HEM142 1.9 45.3 1.0 NA C:HEM142 1.9 49.0 1.0 ND C:HEM142 2.0 45.6 1.0 NE2 C:HIS87 2.1 57.0 1.0 NB C:HEM142 2.1 46.5 1.0 O2 C:OXY150 2.7 50.2 1.0 CE1 C:HIS87 2.9 61.2 1.0 C4C C:HEM142 2.9 43.9 1.0 C1A C:HEM142 2.9 51.5 1.0 C1C C:HEM142 3.0 44.0 1.0 C4A C:HEM142 3.0 49.3 1.0 C1D C:HEM142 3.0 43.9 1.0 C4D C:HEM142 3.0 47.2 1.0 C1B C:HEM142 3.1 48.4 1.0 C4B C:HEM142 3.1 44.7 1.0 CD2 C:HIS87 3.2 64.5 1.0 CHD C:HEM142 3.3 45.8 1.0 CHA C:HEM142 3.4 49.1 1.0 CHB C:HEM142 3.4 50.5 1.0 CHC C:HEM142 3.4 46.5 1.0 ND1 C:HIS87 4.0 65.8 1.0 C3C C:HEM142 4.1 42.8 1.0 C2C C:HEM142 4.2 43.1 1.0 C2A C:HEM142 4.2 54.7 1.0 C3A C:HEM142 4.2 53.1 1.0 CG C:HIS87 4.2 71.2 1.0 C2D C:HEM142 4.3 42.6 1.0 C3D C:HEM142 4.3 45.5 1.0 C2B C:HEM142 4.3 45.1 1.0 C3B C:HEM142 4.3 44.2 1.0 NE2 C:HIS58 4.6 52.6 1.0 CE1 C:HIS58 4.8 54.7 1.0

Iron binding site 4 out of 4 in the T-to-T(High) Quaternary Transitions in Human Hemoglobin: BETAP36A 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: BETAP36A Oxy (2MM Ihp, 20% Peg) (10 Test Sets) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:52.3 occ:1.00 FE D:HEM147 0.0 52.3 1.0 O1 D:OXY150 1.8 47.7 1.0 NB D:HEM147 1.9 53.7 1.0 NC D:HEM147 2.0 52.2 1.0 NA D:HEM147 2.0 57.0 1.0 NE2 D:HIS92 2.1 50.5 1.0 ND D:HEM147 2.1 55.1 1.0 O2 D:OXY150 2.8 49.3 1.0 C1B D:HEM147 2.9 53.5 1.0 C4A D:HEM147 2.9 58.9 1.0 C4C D:HEM147 3.0 52.6 1.0 CE1 D:HIS92 3.0 50.5 1.0 C4B D:HEM147 3.0 54.2 1.0 C1C D:HEM147 3.0 49.5 1.0 C1D D:HEM147 3.1 55.1 1.0 CD2 D:HIS92 3.1 49.7 1.0 C1A D:HEM147 3.1 60.6 1.0 C4D D:HEM147 3.2 58.3 1.0 CHB D:HEM147 3.2 54.8 1.0 CHD D:HEM147 3.3 54.2 1.0 CHC D:HEM147 3.4 52.1 1.0 CHA D:HEM147 3.6 59.7 1.0 ND1 D:HIS92 4.1 49.7 1.0 C2B D:HEM147 4.1 54.2 1.0 C3B D:HEM147 4.2 55.4 1.0 C3C D:HEM147 4.2 51.9 1.0 CG D:HIS92 4.2 50.0 1.0 C2C D:HEM147 4.2 50.0 1.0 C3A D:HEM147 4.2 61.6 1.0 C2A D:HEM147 4.3 64.3 1.0 C2D D:HEM147 4.3 58.0 1.0 C3D D:HEM147 4.4 60.4 1.0 NE2 D:HIS63 4.7 52.2 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