Iron in PDB 1hda: A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin

The structure of A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin, PDB code: 1hda was solved by G.Fermi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.820, 95.510, 105.320, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin (pdb code 1hda). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin, PDB code: 1hda:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe143 b:16.0 occ:1.00 FE A:HEM143 0.0 16.0 1.0 NC A:HEM143 2.0 14.3 1.0 NA A:HEM143 2.0 17.2 1.0 ND A:HEM143 2.0 16.4 1.0 NB A:HEM143 2.0 14.4 1.0 NE2 A:HIS87 2.3 15.4 1.0 C4B A:HEM143 3.1 13.0 1.0 C4D A:HEM143 3.1 17.4 1.0 C1D A:HEM143 3.1 15.8 1.0 C1A A:HEM143 3.1 18.1 1.0 C1C A:HEM143 3.1 13.4 1.0 C4A A:HEM143 3.1 17.4 1.0 C4C A:HEM143 3.1 14.6 1.0 C1B A:HEM143 3.1 13.3 1.0 CE1 A:HIS87 3.2 13.9 1.0 CD2 A:HIS87 3.4 15.2 1.0 CHC A:HEM143 3.4 14.3 1.0 CHA A:HEM143 3.4 17.0 1.0 CHD A:HEM143 3.4 15.3 1.0 CHB A:HEM143 3.5 15.4 1.0 O A:HOH762 3.5 26.8 1.0 C3B A:HEM143 4.3 12.5 1.0 C3D A:HEM143 4.3 18.2 1.0 C2A A:HEM143 4.3 19.6 1.0 C2D A:HEM143 4.3 16.7 1.0 C2B A:HEM143 4.3 12.4 1.0 C3A A:HEM143 4.3 17.2 1.0 C3C A:HEM143 4.3 12.7 1.0 C2C A:HEM143 4.3 12.3 1.0 ND1 A:HIS87 4.3 15.7 1.0 CG A:HIS87 4.5 15.9 1.0 CD1 A:LEU91 4.5 14.8 1.0 NE2 A:HIS58 4.6 19.0 1.0 CE1 A:HIS58 4.7 18.2 1.0

Iron binding site 2 out of 4 in the A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe148 b:14.3 occ:1.00 FE B:HEM148 0.0 14.3 1.0 ND B:HEM148 2.0 16.0 1.0 NC B:HEM148 2.0 14.8 1.0 NA B:HEM148 2.0 14.5 1.0 NB B:HEM148 2.1 13.2 1.0 NE2 B:HIS92 2.3 9.9 1.0 C4C B:HEM148 3.0 14.3 1.0 C1D B:HEM148 3.1 16.3 1.0 C4D B:HEM148 3.1 16.4 1.0 C1A B:HEM148 3.1 14.7 1.0 C4A B:HEM148 3.1 13.6 1.0 C1B B:HEM148 3.1 11.2 1.0 C1C B:HEM148 3.1 13.9 1.0 C4B B:HEM148 3.1 12.2 1.0 CE1 B:HIS92 3.1 11.6 1.0 CD2 B:HIS92 3.3 10.2 1.0 CHA B:HEM148 3.4 15.9 1.0 CHD B:HEM148 3.4 15.2 1.0 CHC B:HEM148 3.4 12.8 1.0 CHB B:HEM148 3.5 11.9 1.0 C3D B:HEM148 4.3 17.5 1.0 NE2 B:HIS63 4.3 17.0 1.0 C3C B:HEM148 4.3 14.0 1.0 C2D B:HEM148 4.3 16.3 1.0 C2C B:HEM148 4.3 14.1 1.0 C3B B:HEM148 4.3 12.2 1.0 C2A B:HEM148 4.3 14.7 1.0 ND1 B:HIS92 4.3 11.2 1.0 C3A B:HEM148 4.3 14.2 1.0 C2B B:HEM148 4.3 11.2 1.0 CG2 B:VAL67 4.3 13.3 1.0 CG B:HIS92 4.4 11.5 1.0 CE1 B:HIS63 4.8 15.6 1.0 CE1 B:PHE103 4.9 20.0 1.0

Iron binding site 3 out of 4 in the A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe143 b:15.4 occ:1.00 FE C:HEM143 0.0 15.4 1.0 ND C:HEM143 2.0 13.1 1.0 NA C:HEM143 2.0 16.5 1.0 NB C:HEM143 2.0 14.2 1.0 NC C:HEM143 2.0 11.4 1.0 NE2 C:HIS87 2.2 14.4 1.0 CE1 C:HIS87 3.0 16.5 1.0 C4D C:HEM143 3.1 12.8 1.0 C1D C:HEM143 3.1 13.3 1.0 C1A C:HEM143 3.1 16.3 1.0 C4A C:HEM143 3.1 16.9 1.0 C4B C:HEM143 3.1 13.4 1.0 C4C C:HEM143 3.1 11.4 1.0 C1C C:HEM143 3.1 10.3 1.0 C1B C:HEM143 3.1 14.2 1.0 CD2 C:HIS87 3.3 16.5 1.0 CHA C:HEM143 3.4 12.4 1.0 CHD C:HEM143 3.4 12.8 1.0 CHB C:HEM143 3.5 15.5 1.0 CHC C:HEM143 3.5 11.8 1.0 O C:HOH761 3.5 22.3 1.0 ND1 C:HIS87 4.2 18.1 1.0 C3D C:HEM143 4.3 13.7 1.0 C2D C:HEM143 4.3 12.7 1.0 C2A C:HEM143 4.3 19.0 1.0 C3A C:HEM143 4.3 18.3 1.0 C3B C:HEM143 4.3 12.9 1.0 C2B C:HEM143 4.3 12.4 1.0 C3C C:HEM143 4.3 10.3 1.0 C2C C:HEM143 4.3 9.8 1.0 CG C:HIS87 4.4 18.6 1.0 CD1 C:LEU91 4.5 18.5 1.0 CE1 C:HIS58 4.5 22.8 1.0 NE2 C:HIS58 4.5 22.7 1.0

Iron binding site 4 out of 4 in the A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe148 b:17.4 occ:1.00 FE D:HEM148 0.0 17.4 1.0 ND D:HEM148 2.0 18.6 1.0 NA D:HEM148 2.0 20.1 1.0 NB D:HEM148 2.0 16.1 1.0 NC D:HEM148 2.0 14.4 1.0 NE2 D:HIS92 2.2 15.4 1.0 C1A D:HEM148 3.0 21.5 1.0 C1B D:HEM148 3.1 15.7 1.0 C1D D:HEM148 3.1 18.9 1.0 C4C D:HEM148 3.1 13.1 1.0 C4D D:HEM148 3.1 19.2 1.0 C1C D:HEM148 3.1 12.1 1.0 C4A D:HEM148 3.1 19.9 1.0 C4B D:HEM148 3.1 14.3 1.0 CE1 D:HIS92 3.2 16.0 1.0 CD2 D:HIS92 3.2 14.8 1.0 CHD D:HEM148 3.4 15.9 1.0 CHC D:HEM148 3.4 12.4 1.0 CHA D:HEM148 3.4 19.8 1.0 CHB D:HEM148 3.5 17.1 1.0 NE2 D:HIS63 4.2 24.6 1.0 C2B D:HEM148 4.3 14.7 1.0 C3B D:HEM148 4.3 14.8 1.0 C2A D:HEM148 4.3 23.3 1.0 C3D D:HEM148 4.3 19.9 1.0 C2D D:HEM148 4.3 19.9 1.0 C2C D:HEM148 4.3 12.0 1.0 C3C D:HEM148 4.3 12.2 1.0 C3A D:HEM148 4.3 21.5 1.0 CG2 D:VAL67 4.3 18.5 1.0 ND1 D:HIS92 4.3 15.6 1.0 CG D:HIS92 4.4 16.1 1.0 CE1 D:HIS63 4.6 24.1 1.0 CD1 D:LEU96 4.9 18.9 1.0

M.F.Perutz, G.Fermi, C.Poyart, J.Pagnier, J.Kister. A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin. J.Mol.Biol. V. 233 536 1993.
ISSN: ISSN 0022-2836
PubMed: 8411160
DOI: 10.1006/JMBI.1993.1530