Iron in PDB 2auq: Hbi (F97V) Co Bound

The structure of Hbi (F97V) Co Bound, PDB code: 2auq was solved by J.E.Knapp, M.A.Bonham, Q.H.Gibson, J.C.Nichols, W.E.Royer Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.59 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	93.110, 43.880, 83.500, 90.00, 121.89, 90.00
R / Rfree (%)	18.2 / 21.4

The binding sites of Iron atom in the Hbi (F97V) Co Bound (pdb code 2auq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Hbi (F97V) Co Bound, PDB code: 2auq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Hbi (F97V) Co Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Hbi (F97V) Co Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe147 b:14.7 occ:1.00 FE A:HEM147 0.0 14.7 1.0 C A:CMO148 1.9 11.1 1.0 NB A:HEM147 2.0 12.6 1.0 ND A:HEM147 2.0 16.0 1.0 NA A:HEM147 2.0 12.0 1.0 NC A:HEM147 2.0 11.9 1.0 NE2 A:HIS101 2.0 12.8 1.0 CE1 A:HIS101 3.0 11.0 1.0 C4D A:HEM147 3.1 16.6 1.0 C1B A:HEM147 3.1 14.9 1.0 C1A A:HEM147 3.1 14.6 1.0 C4B A:HEM147 3.1 13.8 1.0 C1D A:HEM147 3.1 16.6 1.0 C1C A:HEM147 3.1 12.4 1.0 C4C A:HEM147 3.1 16.6 1.0 C4A A:HEM147 3.1 14.3 1.0 CD2 A:HIS101 3.1 13.2 1.0 O A:CMO148 3.1 23.0 1.0 CHA A:HEM147 3.4 14.7 1.0 CHC A:HEM147 3.4 10.9 1.0 CHD A:HEM147 3.4 14.6 1.0 CHB A:HEM147 3.5 13.8 1.0 ND1 A:HIS101 4.2 13.9 1.0 CG A:HIS101 4.2 15.5 1.0 C2B A:HEM147 4.3 14.5 1.0 C3D A:HEM147 4.3 18.5 1.0 C2D A:HEM147 4.3 19.6 1.0 C3B A:HEM147 4.3 17.1 1.0 C2A A:HEM147 4.3 16.6 1.0 C2C A:HEM147 4.3 15.9 1.0 C3A A:HEM147 4.3 16.1 1.0 C3C A:HEM147 4.3 13.9 1.0 CE1 A:HIS69 4.8 22.2 1.0 CD1 A:LEU73 4.9 25.7 1.0 CE1 A:PHE111 4.9 15.2 1.0

Iron binding site 2 out of 2 in the Hbi (F97V) Co Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Hbi (F97V) Co Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:13.9 occ:1.00 FE B:HEM147 0.0 13.9 1.0 C B:CMO148 1.9 13.2 1.0 ND B:HEM147 2.0 13.3 1.0 NB B:HEM147 2.0 11.1 1.0 NA B:HEM147 2.0 16.4 1.0 NC B:HEM147 2.0 14.6 1.0 NE2 B:HIS101 2.1 16.0 1.0 CE1 B:HIS101 3.1 12.3 1.0 C4D B:HEM147 3.1 14.5 1.0 C1A B:HEM147 3.1 15.7 1.0 C1B B:HEM147 3.1 13.4 1.0 C1D B:HEM147 3.1 12.2 1.0 C4A B:HEM147 3.1 15.0 1.0 C1C B:HEM147 3.1 17.0 1.0 C4B B:HEM147 3.1 15.3 1.0 C4C B:HEM147 3.1 14.6 1.0 CD2 B:HIS101 3.1 11.7 1.0 O B:CMO148 3.1 17.8 1.0 CHA B:HEM147 3.4 14.1 1.0 CHB B:HEM147 3.4 16.6 1.0 CHD B:HEM147 3.4 15.5 1.0 CHC B:HEM147 3.4 14.1 1.0 ND1 B:HIS101 4.2 12.9 1.0 CG B:HIS101 4.2 13.7 1.0 C2A B:HEM147 4.3 16.9 1.0 C3D B:HEM147 4.3 15.2 1.0 C2B B:HEM147 4.3 13.8 1.0 C2D B:HEM147 4.3 13.7 1.0 C3A B:HEM147 4.3 16.2 1.0 C2C B:HEM147 4.3 13.9 1.0 C3B B:HEM147 4.3 15.5 1.0 C3C B:HEM147 4.3 14.7 1.0 CE1 B:HIS69 4.9 17.9 1.0 CD1 B:LEU73 5.0 28.0 1.0

J.E.Knapp, M.A.Bonham, Q.H.Gibson, J.C.Nichols, W.E.Royer Jr.. Residue F4 Plays A Key Role in Modulating Oxygen Affinity and Cooperativity in Scapharca Dimeric Hemoglobin Biochemistry V. 44 14419 2005.
ISSN: ISSN 0006-2960
PubMed: 16262242
DOI: 10.1021/BI051052+