Iron in PDB 2av0: F97L with Co Bound

The structure of F97L with Co Bound, PDB code: 2av0 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)	38.43 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	93.250, 43.980, 83.500, 90.00, 122.03, 90.00
R / Rfree (%)	18.9 / 20.6

The binding sites of Iron atom in the F97L with Co Bound (pdb code 2av0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the F97L with Co Bound, PDB code: 2av0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the F97L with Co Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of F97L with Co Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe147 b:14.1 occ:1.00 FE A:HEM147 0.0 14.1 1.0 C A:CMO148 1.9 13.8 1.0 NB A:HEM147 2.0 12.8 1.0 NC A:HEM147 2.0 13.6 1.0 ND A:HEM147 2.0 14.8 1.0 NA A:HEM147 2.0 13.5 1.0 NE2 A:HIS101 2.0 14.0 1.0 C4B A:HEM147 3.0 13.4 1.0 C1C A:HEM147 3.1 13.1 1.0 CE1 A:HIS101 3.1 13.6 1.0 C4D A:HEM147 3.1 15.9 1.0 C1B A:HEM147 3.1 13.7 1.0 CD2 A:HIS101 3.1 14.4 1.0 C1A A:HEM147 3.1 15.2 1.0 C4C A:HEM147 3.1 14.7 1.0 O A:CMO148 3.1 18.0 1.0 C4A A:HEM147 3.1 13.7 1.0 C1D A:HEM147 3.1 15.6 1.0 CHC A:HEM147 3.4 13.6 1.0 CHA A:HEM147 3.4 15.1 1.0 CHD A:HEM147 3.5 15.0 1.0 CHB A:HEM147 3.5 12.8 1.0 ND1 A:HIS101 4.2 14.4 1.0 CG A:HIS101 4.2 14.3 1.0 C2C A:HEM147 4.3 14.2 1.0 C2B A:HEM147 4.3 13.1 1.0 C3B A:HEM147 4.3 13.3 1.0 C2D A:HEM147 4.3 16.2 1.0 C3A A:HEM147 4.3 13.5 1.0 C3D A:HEM147 4.3 17.5 1.0 C2A A:HEM147 4.3 14.0 1.0 C3C A:HEM147 4.3 14.9 1.0 CE1 A:HIS69 4.8 16.5 1.0 CD1 A:LEU73 4.9 18.5 1.0 CE2 A:PHE111 4.9 15.5 1.0

Iron binding site 2 out of 2 in the F97L with Co Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of F97L with Co Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:13.6 occ:1.00 FE B:HEM147 0.0 13.6 1.0 C B:CMO148 1.9 13.9 1.0 ND B:HEM147 2.0 13.7 1.0 NA B:HEM147 2.0 13.2 1.0 NC B:HEM147 2.0 13.9 1.0 NB B:HEM147 2.0 12.4 1.0 NE2 B:HIS101 2.1 12.4 1.0 C1A B:HEM147 3.0 14.0 1.0 C4D B:HEM147 3.0 13.8 1.0 O B:CMO148 3.1 16.2 1.0 C1D B:HEM147 3.1 13.9 1.0 C4B B:HEM147 3.1 12.7 1.0 C4A B:HEM147 3.1 12.6 1.0 C1C B:HEM147 3.1 13.7 1.0 C4C B:HEM147 3.1 14.3 1.0 CE1 B:HIS101 3.1 13.2 1.0 C1B B:HEM147 3.1 12.3 1.0 CD2 B:HIS101 3.1 11.6 1.0 CHA B:HEM147 3.4 13.3 1.0 CHC B:HEM147 3.4 13.9 1.0 CHD B:HEM147 3.4 14.1 1.0 CHB B:HEM147 3.4 12.8 1.0 ND1 B:HIS101 4.2 13.6 1.0 C2A B:HEM147 4.3 14.6 1.0 C3D B:HEM147 4.3 14.3 1.0 CG B:HIS101 4.3 13.9 1.0 C2D B:HEM147 4.3 14.0 1.0 C3A B:HEM147 4.3 13.6 1.0 C2C B:HEM147 4.3 14.2 1.0 C3C B:HEM147 4.3 13.8 1.0 C3B B:HEM147 4.3 12.6 1.0 C2B B:HEM147 4.3 13.1 1.0 CE1 B:HIS69 4.8 15.0 1.0 CD1 B:LEU73 4.9 15.7 1.0 CE1 B:PHE111 5.0 14.9 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+