Iron in PDB 2e2y: Crystal Structure of F43W/H64D/V68I Myoglobin

The structure of Crystal Structure of F43W/H64D/V68I Myoglobin, PDB code: 2e2y was solved by T.Ohki, T.Ueno, T.Hikage, A.Suzuki, T.Yamane, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.34 / 1.60
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	90.651, 90.651, 45.447, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 19.5

The binding sites of Iron atom in the Crystal Structure of F43W/H64D/V68I Myoglobin (pdb code 2e2y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of F43W/H64D/V68I Myoglobin, PDB code: 2e2y:

Iron binding site 1 out of 1 in the Crystal Structure of F43W/H64D/V68I Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of F43W/H64D/V68I Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:13.0 occ:1.00 FE A:HEM154 0.0 13.0 1.0 NC A:HEM154 2.0 10.7 1.0 NA A:HEM154 2.1 11.3 1.0 NB A:HEM154 2.1 11.6 1.0 ND A:HEM154 2.1 12.7 1.0 O A:HOH1224 2.1 13.9 0.4 NE2 A:HIS93 2.1 12.2 1.0 C4C A:HEM154 3.1 12.2 1.0 C1C A:HEM154 3.1 10.7 1.0 C4A A:HEM154 3.1 10.8 1.0 C4B A:HEM154 3.1 10.3 1.0 C1D A:HEM154 3.1 13.0 1.0 CE1 A:HIS93 3.1 13.9 1.0 C1A A:HEM154 3.1 12.8 1.0 C4D A:HEM154 3.1 12.5 1.0 C1B A:HEM154 3.1 10.2 1.0 CD2 A:HIS93 3.2 11.1 1.0 CHD A:HEM154 3.4 12.9 1.0 CHC A:HEM154 3.4 10.5 1.0 CHA A:HEM154 3.4 13.2 1.0 CHB A:HEM154 3.4 11.4 1.0 ND1 A:HIS93 4.2 12.7 1.0 C3C A:HEM154 4.3 12.8 1.0 C2C A:HEM154 4.3 12.1 1.0 CG A:HIS93 4.3 11.6 1.0 C3A A:HEM154 4.3 11.0 1.0 C3B A:HEM154 4.3 10.7 1.0 C2B A:HEM154 4.3 10.2 1.0 C2A A:HEM154 4.3 12.3 1.0 C2D A:HEM154 4.3 13.0 1.0 C3D A:HEM154 4.3 14.8 1.0 CG1 A:ILE68 4.4 8.1 1.0 O A:HOH1119 4.5 39.1 1.0 CD1 A:ILE68 4.6 10.6 1.0 CH2 A:TRP43 4.8 24.5 1.0 CZ2 A:TRP43 4.8 24.6 1.0

Y.Watanabe, H.Nakajima, T.Ueno. Reactivities of Oxo and Peroxo Intermediates Studied By Hemoprotein Mutants Acc.Chem.Res. V. 40 554 2007.
ISSN: ISSN 0001-4842
PubMed: 17567089
DOI: 10.1021/AR600046A