Iron in PDB 1faw: Graylag Goose Hemoglobin (Oxy Form)

The structure of Graylag Goose Hemoglobin (Oxy Form), PDB code: 1faw was solved by Y.-H.Liang, X.-Z.Liu, S.-H.Liu, G.-Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.30 / 3.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.552, 80.624, 72.571, 90.00, 102.75, 90.00
R / Rfree (%)	17.6 / 22

The binding sites of Iron atom in the Graylag Goose Hemoglobin (Oxy Form) (pdb code 1faw). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Graylag Goose Hemoglobin (Oxy Form), PDB code: 1faw:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Graylag 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 Graylag Goose Hemoglobin (Oxy Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:23.6 occ:1.00 FE A:HEM150 0.0 23.6 1.0 O1 A:OXY151 1.7 43.2 1.0 NA A:HEM150 1.9 20.7 1.0 ND A:HEM150 2.0 20.7 1.0 NB A:HEM150 2.0 20.7 1.0 NC A:HEM150 2.0 20.7 1.0 NE2 A:HIS87 2.2 19.4 1.0 O2 A:OXY151 2.9 43.2 1.0 C1A A:HEM150 3.0 20.7 1.0 C4A A:HEM150 3.0 20.7 1.0 C4B A:HEM150 3.0 20.7 1.0 C1D A:HEM150 3.0 20.7 1.0 C1C A:HEM150 3.0 20.7 1.0 C4D A:HEM150 3.0 20.7 1.0 C1B A:HEM150 3.1 20.7 1.0 C4C A:HEM150 3.1 20.7 1.0 CE1 A:HIS87 3.1 19.4 1.0 CD2 A:HIS87 3.2 19.4 1.0 CHC A:HEM150 3.4 20.7 1.0 CHA A:HEM150 3.4 20.7 1.0 CHB A:HEM150 3.4 20.7 1.0 CHD A:HEM150 3.4 20.7 1.0 C2A A:HEM150 4.2 20.7 1.0 C3A A:HEM150 4.3 20.7 1.0 C3D A:HEM150 4.3 20.7 1.0 C2D A:HEM150 4.3 20.7 1.0 C2C A:HEM150 4.3 20.7 1.0 C3B A:HEM150 4.3 20.7 1.0 C2B A:HEM150 4.3 20.7 1.0 C3C A:HEM150 4.3 20.7 1.0 CG A:HIS87 4.3 19.4 1.0 ND1 A:HIS87 4.3 19.4 1.0 NE2 A:HIS58 4.5 19.0 1.0 CE1 A:HIS58 4.8 19.0 1.0

Iron binding site 2 out of 4 in the Graylag 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 Graylag Goose Hemoglobin (Oxy Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:27.6 occ:1.00 FE B:HEM150 0.0 27.6 1.0 O1 B:OXY151 1.7 36.9 1.0 NC B:HEM150 2.0 22.9 1.0 NB B:HEM150 2.0 22.9 1.0 ND B:HEM150 2.0 22.9 1.0 NA B:HEM150 2.0 22.9 1.0 NE2 B:HIS92 2.1 19.7 1.0 O2 B:OXY151 2.8 36.9 1.0 C1C B:HEM150 3.0 22.9 1.0 C1B B:HEM150 3.0 22.9 1.0 C4A B:HEM150 3.0 22.9 1.0 C4C B:HEM150 3.0 22.9 1.0 C1D B:HEM150 3.0 22.9 1.0 C4B B:HEM150 3.0 22.9 1.0 C1A B:HEM150 3.1 22.9 1.0 C4D B:HEM150 3.1 22.9 1.0 CE1 B:HIS92 3.1 19.7 1.0 CD2 B:HIS92 3.1 19.7 1.0 CHB B:HEM150 3.4 22.9 1.0 CHC B:HEM150 3.4 22.9 1.0 CHD B:HEM150 3.4 22.9 1.0 CHA B:HEM150 3.4 22.9 1.0 CG B:HIS92 4.2 19.7 1.0 ND1 B:HIS92 4.2 19.7 1.0 C2B B:HEM150 4.3 22.9 1.0 C2C B:HEM150 4.3 22.9 1.0 C2A B:HEM150 4.3 22.9 1.0 C3A B:HEM150 4.3 22.9 1.0 C3C B:HEM150 4.3 22.9 1.0 C2D B:HEM150 4.3 22.9 1.0 C3B B:HEM150 4.3 22.9 1.0 C3D B:HEM150 4.3 22.9 1.0 NE2 B:HIS63 4.4 15.9 1.0 CE1 B:HIS63 4.9 15.9 1.0 CG2 B:VAL67 4.9 12.1 1.0

Iron binding site 3 out of 4 in the Graylag Goose Hemoglobin (Oxy Form)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Graylag Goose Hemoglobin (Oxy Form) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe150 b:23.6 occ:1.00 FE C:HEM150 0.0 23.6 1.0 O1 C:OXY151 1.7 43.2 1.0 NA C:HEM150 1.9 20.7 1.0 ND C:HEM150 2.0 20.7 1.0 NB C:HEM150 2.0 20.7 1.0 NC C:HEM150 2.0 20.7 1.0 NE2 C:HIS87 2.2 19.4 1.0 O2 C:OXY151 2.9 43.2 1.0 C1A C:HEM150 3.0 20.7 1.0 C4A C:HEM150 3.0 20.7 1.0 C4B C:HEM150 3.0 20.7 1.0 C1D C:HEM150 3.0 20.7 1.0 C1C C:HEM150 3.0 20.7 1.0 C4D C:HEM150 3.0 20.7 1.0 C1B C:HEM150 3.1 20.7 1.0 C4C C:HEM150 3.1 20.7 1.0 CE1 C:HIS87 3.1 19.4 1.0 CD2 C:HIS87 3.2 19.4 1.0 CHC C:HEM150 3.4 20.7 1.0 CHA C:HEM150 3.4 20.7 1.0 CHD C:HEM150 3.4 20.7 1.0 CHB C:HEM150 3.4 20.7 1.0 C2A C:HEM150 4.2 20.7 1.0 C3A C:HEM150 4.3 20.7 1.0 C3D C:HEM150 4.3 20.7 1.0 C2D C:HEM150 4.3 20.7 1.0 C2C C:HEM150 4.3 20.7 1.0 C3B C:HEM150 4.3 20.7 1.0 C2B C:HEM150 4.3 20.7 1.0 C3C C:HEM150 4.3 20.7 1.0 CG C:HIS87 4.3 19.4 1.0 ND1 C:HIS87 4.3 19.4 1.0 NE2 C:HIS58 4.5 19.0 1.0 CE1 C:HIS58 4.8 19.0 1.0

Iron binding site 4 out of 4 in the Graylag Goose Hemoglobin (Oxy Form)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Graylag Goose Hemoglobin (Oxy Form) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe150 b:27.6 occ:1.00 FE D:HEM150 0.0 27.6 1.0 O1 D:OXY151 1.7 36.9 1.0 NC D:HEM150 2.0 22.9 1.0 NB D:HEM150 2.0 22.9 1.0 ND D:HEM150 2.0 22.9 1.0 NA D:HEM150 2.0 22.9 1.0 NE2 D:HIS92 2.1 19.7 1.0 O2 D:OXY151 2.8 36.9 1.0 C1C D:HEM150 3.0 22.9 1.0 C1B D:HEM150 3.0 22.9 1.0 C4A D:HEM150 3.0 22.9 1.0 C4C D:HEM150 3.0 22.9 1.0 C1D D:HEM150 3.0 22.9 1.0 C4B D:HEM150 3.0 22.9 1.0 C1A D:HEM150 3.1 22.9 1.0 C4D D:HEM150 3.1 22.9 1.0 CE1 D:HIS92 3.1 19.7 1.0 CD2 D:HIS92 3.1 19.7 1.0 CHB D:HEM150 3.4 22.9 1.0 CHC D:HEM150 3.4 22.9 1.0 CHD D:HEM150 3.4 22.9 1.0 CHA D:HEM150 3.4 22.9 1.0 CG D:HIS92 4.2 19.7 1.0 ND1 D:HIS92 4.2 19.7 1.0 C2B D:HEM150 4.3 22.9 1.0 C2C D:HEM150 4.3 22.9 1.0 C2A D:HEM150 4.3 22.9 1.0 C3A D:HEM150 4.3 22.9 1.0 C3C D:HEM150 4.3 22.9 1.0 C2D D:HEM150 4.3 22.9 1.0 C3B D:HEM150 4.3 22.9 1.0 C3D D:HEM150 4.3 22.9 1.0 NE2 D:HIS63 4.4 15.9 1.0 CE1 D:HIS63 4.9 15.9 1.0 CG2 D:VAL67 4.9 12.1 1.0

Y.H.Liang, X.Z.Liu, S.H.Liu, G.Y.Lu. The Structure of Greylag Goose Oxy Haemoglobin: the Roles of Four Mutations Compared with Bar-Headed Goose Haemoglobin. Acta Crystallogr.,Sect.D V. 57 1850 2001.
ISSN: ISSN 0907-4449
PubMed: 11717498
DOI: 10.1107/S0907444901016493