Iron in PDB 1lfq: Oxy Hemoglobin (93% Relative Humidity)

The structure of Oxy Hemoglobin (93% Relative Humidity), PDB code: 1lfq was solved by B.K.Biswal, M.Vijayan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	54.200, 54.200, 195.700, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 25.8

The binding sites of Iron atom in the Oxy Hemoglobin (93% Relative Humidity) (pdb code 1lfq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Oxy Hemoglobin (93% Relative Humidity), PDB code: 1lfq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Oxy Hemoglobin (93% Relative Humidity)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxy Hemoglobin (93% Relative Humidity) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:34.2 occ:1.00 FE A:HEM142 0.0 34.2 1.0 ND A:HEM142 2.0 34.2 1.0 NA A:HEM142 2.0 34.2 1.0 NB A:HEM142 2.0 34.2 1.0 NC A:HEM142 2.0 34.2 1.0 NE2 A:HIS87 2.2 24.2 1.0 CE1 A:HIS87 2.9 24.2 1.0 C4D A:HEM142 3.0 34.2 1.0 C1A A:HEM142 3.0 34.2 1.0 C1C A:HEM142 3.1 34.2 1.0 C1D A:HEM142 3.1 34.2 1.0 C4B A:HEM142 3.1 34.2 1.0 C4A A:HEM142 3.1 34.2 1.0 C1B A:HEM142 3.1 34.2 1.0 C4C A:HEM142 3.1 34.2 1.0 CD2 A:HIS87 3.4 24.2 1.0 CHA A:HEM142 3.4 34.2 1.0 CHC A:HEM142 3.4 34.2 1.0 CHB A:HEM142 3.5 34.2 1.0 CHD A:HEM142 3.5 34.2 1.0 ND1 A:HIS87 4.1 24.2 1.0 NE2 A:HIS58 4.1 18.7 1.0 C3D A:HEM142 4.2 34.2 1.0 C2D A:HEM142 4.3 34.2 1.0 C2A A:HEM142 4.3 34.2 1.0 C3A A:HEM142 4.3 34.2 1.0 C2C A:HEM142 4.3 34.2 1.0 C3B A:HEM142 4.3 34.2 1.0 C2B A:HEM142 4.3 34.2 1.0 C3C A:HEM142 4.3 34.2 1.0 CG A:HIS87 4.4 24.2 1.0 CE1 A:HIS58 4.6 18.7 1.0

Iron binding site 2 out of 2 in the Oxy Hemoglobin (93% Relative Humidity)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Oxy Hemoglobin (93% Relative Humidity) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:34.2 occ:1.00 FE B:HEM147 0.0 34.2 1.0 NA B:HEM147 2.0 34.2 1.0 NB B:HEM147 2.0 34.2 1.0 ND B:HEM147 2.0 34.2 1.0 NC B:HEM147 2.1 34.2 1.0 NE2 B:HIS92 2.2 24.1 1.0 C1A B:HEM147 3.0 34.2 1.0 C4D B:HEM147 3.0 34.2 1.0 C4A B:HEM147 3.0 34.2 1.0 C4B B:HEM147 3.0 34.2 1.0 C1B B:HEM147 3.0 34.2 1.0 C1D B:HEM147 3.1 34.2 1.0 CE1 B:HIS92 3.1 24.1 1.0 C1C B:HEM147 3.1 34.2 1.0 C4C B:HEM147 3.1 34.2 1.0 CD2 B:HIS92 3.2 24.1 1.0 CHA B:HEM147 3.4 34.2 1.0 CHB B:HEM147 3.4 34.2 1.0 CHC B:HEM147 3.4 34.2 1.0 CHD B:HEM147 3.5 34.2 1.0 NE2 B:HIS63 4.2 31.9 1.0 C3D B:HEM147 4.2 34.2 1.0 C2A B:HEM147 4.2 34.2 1.0 ND1 B:HIS92 4.2 24.1 1.0 C3A B:HEM147 4.2 34.2 1.0 C2D B:HEM147 4.2 34.2 1.0 C2B B:HEM147 4.3 34.2 1.0 C3B B:HEM147 4.3 34.2 1.0 CG B:HIS92 4.3 24.1 1.0 C2C B:HEM147 4.4 34.2 1.0 C3C B:HEM147 4.4 34.2 1.0 CG2 B:VAL67 4.7 30.6 1.0 CE1 B:HIS63 4.9 31.9 1.0

B.K.Biswal, M.Vijayan. Structures of Human Oxy- and Deoxyhaemoglobin at Different Levels of Humidity: Variability in the T State. Acta Crystallogr.,Sect.D V. 58 1155 2002.
ISSN: ISSN 0907-4449
PubMed: 12077435
DOI: 10.1107/S0907444902007138