Iron in PDB 2hhe: Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin

The structure of Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin, PDB code: 2hhe was solved by G.L.Gilliland, I.Pechik, C.Fronticelli, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.710, 82.380, 53.580, 90.00, 99.21, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin (pdb code 2hhe). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin, PDB code: 2hhe:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:14.6 occ:1.00 FE A:HEM142 0.0 14.6 1.0 NC A:HEM142 2.0 11.9 1.0 ND A:HEM142 2.0 12.2 1.0 NA A:HEM142 2.0 13.2 1.0 NB A:HEM142 2.0 13.7 1.0 NE2 A:HIS87 2.4 18.5 1.0 C1A A:HEM142 3.0 13.2 1.0 C1D A:HEM142 3.0 12.2 1.0 C4C A:HEM142 3.0 11.2 1.0 C4D A:HEM142 3.0 13.2 1.0 C1C A:HEM142 3.1 12.2 1.0 C4B A:HEM142 3.1 13.6 1.0 O A:HOH147 3.1 13.7 1.0 C4A A:HEM142 3.1 13.1 1.0 C1B A:HEM142 3.1 13.2 1.0 CE1 A:HIS87 3.1 18.2 1.0 CHD A:HEM142 3.4 11.1 1.0 CHC A:HEM142 3.4 13.2 1.0 CHB A:HEM142 3.5 13.1 1.0 CHA A:HEM142 3.5 12.8 1.0 CD2 A:HIS87 3.6 18.0 1.0 C2A A:HEM142 4.3 13.0 1.0 C2D A:HEM142 4.3 12.9 1.0 C2C A:HEM142 4.3 11.5 1.0 C3B A:HEM142 4.3 13.8 1.0 C2B A:HEM142 4.3 13.3 1.0 C3A A:HEM142 4.3 12.8 1.0 C3C A:HEM142 4.3 10.6 1.0 C3D A:HEM142 4.3 13.2 1.0 NE2 A:HIS58 4.3 10.0 1.0 ND1 A:HIS87 4.3 18.1 1.0 CE1 A:HIS58 4.5 10.1 1.0 CG A:HIS87 4.6 19.1 1.0 CD1 A:LEU91 4.8 17.2 1.0

Iron binding site 2 out of 4 in the Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:10.2 occ:1.00 FE B:HEM147 0.0 10.2 1.0 ND B:HEM147 2.0 8.1 1.0 NB B:HEM147 2.0 6.5 1.0 NC B:HEM147 2.0 5.7 1.0 NA B:HEM147 2.0 8.7 1.0 NE2 B:HIS92 2.4 17.1 1.0 C4D B:HEM147 3.0 9.3 1.0 C4B B:HEM147 3.0 6.1 1.0 C1C B:HEM147 3.0 5.7 1.0 C4A B:HEM147 3.1 9.1 1.0 C1D B:HEM147 3.1 8.4 1.0 C1B B:HEM147 3.1 6.9 1.0 C1A B:HEM147 3.1 9.8 1.0 C4C B:HEM147 3.1 6.1 1.0 CD2 B:HIS92 3.2 16.1 1.0 CHA B:HEM147 3.3 9.5 1.0 CE1 B:HIS92 3.4 17.1 1.0 CHC B:HEM147 3.4 6.1 1.0 CHB B:HEM147 3.5 8.2 1.0 CG2 B:VAL67 3.5 19.5 1.0 CHD B:HEM147 3.5 7.2 1.0 NE2 B:HIS63 4.2 25.6 1.0 C3D B:HEM147 4.2 9.7 1.0 C2A B:HEM147 4.3 11.1 1.0 C2D B:HEM147 4.3 8.7 1.0 C2C B:HEM147 4.3 5.5 1.0 C3B B:HEM147 4.3 5.5 1.0 C3A B:HEM147 4.3 10.1 1.0 C2B B:HEM147 4.3 5.8 1.0 C3C B:HEM147 4.3 5.9 1.0 CG B:HIS92 4.4 17.6 1.0 ND1 B:HIS92 4.4 16.6 1.0 CB B:VAL67 4.8 20.3 1.0 CE1 B:HIS63 4.8 24.9 1.0 CD1 B:LEU96 4.9 11.0 1.0

Iron binding site 3 out of 4 in the Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:10.2 occ:1.00 FE C:HEM142 0.0 10.2 1.0 NC C:HEM142 2.0 5.8 1.0 ND C:HEM142 2.0 7.1 1.0 NA C:HEM142 2.0 9.1 1.0 NB C:HEM142 2.1 7.9 1.0 NE2 C:HIS87 2.5 13.7 1.0 C1D C:HEM142 3.0 7.3 1.0 C4C C:HEM142 3.0 6.5 1.0 C1C C:HEM142 3.0 6.4 1.0 C4D C:HEM142 3.0 7.7 1.0 C4A C:HEM142 3.0 9.3 1.0 C1A C:HEM142 3.1 10.0 1.0 C1B C:HEM142 3.1 7.4 1.0 C4B C:HEM142 3.1 7.2 1.0 CD2 C:HIS87 3.3 13.7 1.0 CHD C:HEM142 3.4 6.8 1.0 CHC C:HEM142 3.4 7.0 1.0 CE1 C:HIS87 3.4 14.0 1.0 CHA C:HEM142 3.4 9.2 1.0 CHB C:HEM142 3.5 8.4 1.0 O C:HOH144 3.6 9.6 0.9 CE1 C:HIS58 4.1 11.0 1.0 C3D C:HEM142 4.2 7.5 1.0 C2D C:HEM142 4.2 7.4 1.0 C3C C:HEM142 4.2 6.0 1.0 C2C C:HEM142 4.2 5.9 1.0 C2A C:HEM142 4.3 10.1 1.0 C3A C:HEM142 4.3 9.9 1.0 C3B C:HEM142 4.3 7.5 1.0 C2B C:HEM142 4.3 7.5 1.0 NE2 C:HIS58 4.4 11.0 1.0 CD1 C:LEU91 4.5 15.7 1.0 ND1 C:HIS87 4.5 13.7 1.0 CG C:HIS87 4.5 14.9 1.0

Iron binding site 4 out of 4 in the Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Oxygen Affinity Modulation By the N-Termini of the Beta Chains in Human and Bovine Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:12.8 occ:1.00 FE D:HEM147 0.0 12.8 1.0 ND D:HEM147 2.0 11.9 1.0 NB D:HEM147 2.0 10.2 1.0 NA D:HEM147 2.0 12.6 1.0 NC D:HEM147 2.0 10.2 1.0 NE2 D:HIS92 2.4 19.1 1.0 C1B D:HEM147 3.0 10.5 1.0 C4D D:HEM147 3.0 13.1 1.0 C4B D:HEM147 3.0 9.9 1.0 C1D D:HEM147 3.0 12.4 1.0 C1A D:HEM147 3.1 13.2 1.0 C4A D:HEM147 3.1 12.9 1.0 C4C D:HEM147 3.1 10.1 1.0 CD2 D:HIS92 3.1 19.4 1.0 C1C D:HEM147 3.1 9.7 1.0 CHB D:HEM147 3.4 11.7 1.0 CHA D:HEM147 3.4 13.0 1.0 CHD D:HEM147 3.5 10.8 1.0 CHC D:HEM147 3.5 9.4 1.0 CE1 D:HIS92 3.5 20.3 1.0 CE1 D:HIS63 4.2 25.2 1.0 C2B D:HEM147 4.2 9.9 1.0 C3B D:HEM147 4.3 9.4 1.0 C3D D:HEM147 4.3 13.4 1.0 C2D D:HEM147 4.3 12.8 1.0 C2A D:HEM147 4.3 14.4 1.0 C3A D:HEM147 4.3 13.3 1.0 NE2 D:HIS63 4.3 25.4 1.0 C2C D:HEM147 4.3 9.6 1.0 C3C D:HEM147 4.3 10.1 1.0 CG D:HIS92 4.3 20.0 1.0 CG2 D:VAL67 4.4 17.2 1.0 ND1 D:HIS92 4.5 19.2 1.0 CD1 D:LEU96 4.8 11.5 1.0

C.Fronticelli, I.Pechik, W.S.Brinigar, J.Kowalczyk, G.L.Gilliland. Chloride Ion Independence of the Bohr Effect in A Mutant Human Hemoglobin Beta (V1M+H2DELETED). J.Biol.Chem. V. 269 23965 1994.
ISSN: ISSN 0021-9258
PubMed: 7929044