Iron in PDB 1tes: Oxygen Binding Muscle Protein

The structure of Oxygen Binding Muscle Protein, PDB code: 1tes was solved by R.D.Smith, G.N.Phillips Jr., J.S.Olson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.70
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.622, 91.622, 45.963, 90.00, 90.00, 120.00
R / Rfree (%)	15.9 / n/a

The binding sites of Iron atom in the Oxygen Binding Muscle Protein (pdb code 1tes). 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 Oxygen Binding Muscle Protein, PDB code: 1tes:

Iron binding site 1 out of 1 in the Oxygen Binding Muscle Protein


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxygen Binding Muscle Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe155 b:15.3 occ:1.00 FE A:HEM155 0.0 15.3 1.0 NA A:HEM155 1.9 14.5 1.0 NB A:HEM155 1.9 14.1 1.0 NC A:HEM155 2.0 14.7 1.0 C A:ETN156 2.1 14.8 0.9 ND A:HEM155 2.1 15.2 1.0 NE2 A:HIS94 2.2 14.8 1.0 C1B A:HEM155 2.9 14.2 1.0 C4A A:HEM155 2.9 14.3 1.0 C4B A:HEM155 3.0 13.7 1.0 C1C A:HEM155 3.0 14.5 1.0 C1A A:HEM155 3.0 15.0 1.0 C4C A:HEM155 3.1 14.9 1.0 C1D A:HEM155 3.1 15.4 1.0 N A:ETN156 3.1 15.2 0.9 C4D A:HEM155 3.1 15.9 1.0 CD2 A:HIS94 3.1 15.0 1.0 CE1 A:HIS94 3.2 15.3 1.0 CHB A:HEM155 3.3 14.3 1.0 CHC A:HEM155 3.4 14.1 1.0 CHD A:HEM155 3.4 14.5 1.0 CHA A:HEM155 3.5 16.0 1.0 C3B A:HEM155 4.2 13.9 1.0 C2B A:HEM155 4.2 14.5 1.0 C2A A:HEM155 4.3 15.7 1.0 CG A:HIS94 4.3 15.0 1.0 C2C A:HEM155 4.3 14.9 1.0 C3A A:HEM155 4.3 14.9 1.0 C3C A:HEM155 4.3 15.3 1.0 C1 A:ETN156 4.3 15.8 0.9 ND1 A:HIS94 4.4 15.4 1.0 C2D A:HEM155 4.4 16.5 1.0 C3D A:HEM155 4.4 16.9 1.0 C2 A:ETN156 4.6 15.8 0.9 NE2 A:HIS65 4.7 17.3 1.0 CG2 A:VAL69 4.7 14.6 1.0

R.F.Eich, T.Li, D.D.Lemon, D.H.Doherty, S.R.Curry, J.F.Aitken, A.J.Mathews, K.A.Johnson, R.D.Smith, G.N.Phillips Jr., J.S.Olson. Mechanism of No-Induced Oxidation of Myoglobin and Hemoglobin. Biochemistry V. 35 6976 1996.
ISSN: ISSN 0006-2960
PubMed: 8679521
DOI: 10.1021/BI960442G