Iron in PDB 3pel: Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity

The structure of Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity, PDB code: 3pel was solved by V.S.Bhatt, S.Zaldivar-Lopez, D.R.Harris, C.G.Couto, P.G.Wang, A.F.Palmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.50 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	87.973, 88.045, 53.073, 90.00, 103.37, 90.00
R / Rfree (%)	18.8 / 23.2

The binding sites of Iron atom in the Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity (pdb code 3pel). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity, PDB code: 3pel:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:10.9 occ:1.00 FE A:HEM142 0.0 10.9 1.0 NA A:HEM142 2.1 10.9 1.0 NB A:HEM142 2.1 10.5 1.0 NC A:HEM142 2.1 10.3 1.0 ND A:HEM142 2.1 10.6 1.0 NE2 A:HIS87 2.1 11.7 1.0 O A:HOH451 2.4 30.0 1.0 C1C A:HEM142 3.1 10.4 1.0 C4D A:HEM142 3.1 11.2 1.0 C4B A:HEM142 3.1 10.7 1.0 C1A A:HEM142 3.1 11.8 1.0 C4A A:HEM142 3.1 11.0 1.0 C1B A:HEM142 3.1 10.5 1.0 C4C A:HEM142 3.1 10.2 1.0 C1D A:HEM142 3.1 10.7 1.0 CE1 A:HIS87 3.1 11.2 1.0 CD2 A:HIS87 3.1 11.3 1.0 CHA A:HEM142 3.4 11.4 1.0 CHC A:HEM142 3.4 10.2 1.0 CHB A:HEM142 3.5 11.0 1.0 CHD A:HEM142 3.5 10.4 1.0 ND1 A:HIS87 4.2 11.3 1.0 CG A:HIS87 4.3 11.7 1.0 C2C A:HEM142 4.3 10.2 1.0 C2A A:HEM142 4.3 12.5 1.0 C3B A:HEM142 4.3 10.4 1.0 C3A A:HEM142 4.3 11.8 1.0 C3C A:HEM142 4.3 10.3 1.0 C2B A:HEM142 4.3 10.6 1.0 C3D A:HEM142 4.3 11.4 1.0 NE2 A:HIS58 4.3 13.8 1.0 C2D A:HEM142 4.3 11.3 1.0 CE1 A:HIS58 4.4 14.3 1.0

Iron binding site 2 out of 2 in the Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:16.4 occ:1.00 FE B:HEM147 0.0 16.4 1.0 NC B:HEM147 2.0 16.2 1.0 NB B:HEM147 2.1 16.4 1.0 NA B:HEM147 2.1 17.1 1.0 ND B:HEM147 2.1 16.6 1.0 O B:HOH452 2.2 30.0 1.0 NE2 B:HIS92 2.2 21.1 1.0 C1C B:HEM147 3.0 16.1 1.0 C4C B:HEM147 3.1 16.2 1.0 C1A B:HEM147 3.1 17.7 1.0 C4B B:HEM147 3.1 16.7 1.0 C4D B:HEM147 3.1 17.0 1.0 C1D B:HEM147 3.1 16.5 1.0 C4A B:HEM147 3.1 17.1 1.0 C1B B:HEM147 3.1 16.6 1.0 CE1 B:HIS92 3.1 21.5 1.0 CD2 B:HIS92 3.2 21.6 1.0 CHC B:HEM147 3.4 16.3 1.0 CHA B:HEM147 3.4 17.4 1.0 CHD B:HEM147 3.4 16.5 1.0 CHB B:HEM147 3.5 16.8 1.0 NE2 B:HIS63 4.2 17.0 1.0 C2C B:HEM147 4.3 16.0 1.0 ND1 B:HIS92 4.3 21.4 1.0 C3C B:HEM147 4.3 16.1 1.0 C2A B:HEM147 4.3 18.6 1.0 C3B B:HEM147 4.3 16.8 1.0 C3A B:HEM147 4.3 17.9 1.0 C3D B:HEM147 4.3 17.4 1.0 C2B B:HEM147 4.3 16.6 1.0 C2D B:HEM147 4.3 17.1 1.0 CG B:HIS92 4.4 22.5 1.0 CG2 B:VAL67 4.8 16.5 1.0 CE1 B:HIS63 4.8 17.4 1.0

V.S.Bhatt, S.Zaldivar-Lopez, D.R.Harris, C.G.Couto, P.G.Wang, A.F.Palmer. Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity. Acta Crystallogr.,Sect.D V. 67 395 2011.
ISSN: ISSN 0907-4449
PubMed: 21543841
DOI: 10.1107/S0907444911006044