Iron in PDB 1a4f: Bar-Headed Goose Hemoglobin (Oxy Form)

The structure of Bar-Headed Goose Hemoglobin (Oxy Form), PDB code: 1a4f was solved by J.Zhang, X.Gu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.590, 81.590, 107.280, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Bar-Headed Goose Hemoglobin (Oxy Form) (pdb code 1a4f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Bar-Headed Goose Hemoglobin (Oxy Form), PDB code: 1a4f:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Bar-Headed Goose Hemoglobin (Oxy Form)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bar-Headed Goose Hemoglobin (Oxy Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:23.5 occ:1.00 FE A:HEM150 0.0 23.5 1.0 O1 A:OXY151 1.8 18.1 1.0 NA A:HEM150 2.0 26.1 1.0 ND A:HEM150 2.0 28.5 1.0 NC A:HEM150 2.0 24.4 1.0 NB A:HEM150 2.1 22.8 1.0 NE2 A:HIS87 2.1 8.6 1.0 CD2 A:HIS87 2.9 20.8 1.0 O2 A:OXY151 3.0 43.8 1.0 C1A A:HEM150 3.0 29.1 1.0 C4D A:HEM150 3.0 25.0 1.0 C4A A:HEM150 3.0 34.9 1.0 C1B A:HEM150 3.1 22.6 1.0 C4C A:HEM150 3.1 17.2 1.0 C4B A:HEM150 3.1 19.6 1.0 C1C A:HEM150 3.1 16.8 1.0 C1D A:HEM150 3.1 24.9 1.0 CE1 A:HIS87 3.3 17.6 1.0 CHA A:HEM150 3.3 26.4 1.0 CHC A:HEM150 3.5 22.1 1.0 CHB A:HEM150 3.5 27.6 1.0 CHD A:HEM150 3.5 27.2 1.0 CG A:HIS87 4.2 15.5 1.0 C2A A:HEM150 4.2 27.6 1.0 C3A A:HEM150 4.2 22.4 1.0 C3D A:HEM150 4.3 27.1 1.0 C2B A:HEM150 4.3 24.2 1.0 C3B A:HEM150 4.3 19.8 1.0 ND1 A:HIS87 4.3 21.2 1.0 C3C A:HEM150 4.3 19.2 1.0 C2C A:HEM150 4.3 17.1 1.0 C2D A:HEM150 4.3 23.3 1.0 NE2 A:HIS58 4.5 21.7 1.0 CE1 A:HIS58 4.8 26.5 1.0

Iron binding site 2 out of 2 in the Bar-Headed Goose Hemoglobin (Oxy Form)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Bar-Headed Goose Hemoglobin (Oxy Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:19.8 occ:1.00 FE B:HEM150 0.0 19.8 1.0 O1 B:OXY151 1.8 18.8 1.0 ND B:HEM150 2.0 16.7 1.0 NC B:HEM150 2.0 19.2 1.0 NA B:HEM150 2.0 18.7 1.0 NB B:HEM150 2.0 19.2 1.0 NE2 B:HIS92 2.1 13.1 1.0 C4D B:HEM150 3.0 17.8 1.0 O2 B:OXY151 3.0 28.5 1.0 C4C B:HEM150 3.0 11.2 1.0 C1A B:HEM150 3.0 17.6 1.0 C1B B:HEM150 3.0 18.9 1.0 C4B B:HEM150 3.1 16.9 1.0 CE1 B:HIS92 3.1 18.0 1.0 C1C B:HEM150 3.1 15.2 1.0 C1D B:HEM150 3.1 14.3 1.0 C4A B:HEM150 3.1 16.2 1.0 CD2 B:HIS92 3.1 11.7 1.0 CHA B:HEM150 3.3 16.5 1.0 CHC B:HEM150 3.4 17.2 1.0 CHD B:HEM150 3.4 18.4 1.0 CHB B:HEM150 3.5 16.4 1.0 ND1 B:HIS92 4.2 16.9 1.0 CG B:HIS92 4.2 17.6 1.0 C3C B:HEM150 4.2 9.8 1.0 C3D B:HEM150 4.2 16.6 1.0 C2A B:HEM150 4.2 14.7 1.0 C2C B:HEM150 4.3 7.4 1.0 C2B B:HEM150 4.3 12.5 1.0 C2D B:HEM150 4.3 13.4 1.0 C3A B:HEM150 4.3 17.7 1.0 C3B B:HEM150 4.3 17.1 1.0 NE2 B:HIS63 4.5 12.9 1.0 CG2 B:VAL67 4.9 18.8 1.0 CE1 B:HIS63 5.0 15.2 1.0

J.Zhang, Z.Hua, J.R.Tame, G.Lu, R.Zhang, X.Gu. The Crystal Structure of A High Oxygen Affinity Species of Haemoglobin (Bar-Headed Goose Haemoglobin in the Oxy Form). J.Mol.Biol. V. 255 484 1996.
ISSN: ISSN 0022-2836
PubMed: 8568892
DOI: 10.1006/JMBI.1996.0040