Iron in PDB 2nsr: Nitromethane Modified Horse Heart Myoglobin

The structure of Nitromethane Modified Horse Heart Myoglobin, PDB code: 2nsr was solved by D.M.Copeland, A.H.West, G.B.Richter-Addo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.93 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	35.344, 28.740, 63.471, 90.00, 106.00, 90.00
R / Rfree (%)	16 / 23.1

The binding sites of Iron atom in the Nitromethane Modified Horse Heart Myoglobin (pdb code 2nsr). 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 Nitromethane Modified Horse Heart Myoglobin, PDB code: 2nsr:

Iron binding site 1 out of 1 in the Nitromethane Modified Horse Heart Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nitromethane Modified Horse Heart Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:16.4 occ:1.00 FE A:HEM154 0.0 16.4 1.0 N A:NSM155 2.0 14.9 0.8 NC A:HEM154 2.0 12.5 1.0 NB A:HEM154 2.1 13.8 1.0 ND A:HEM154 2.1 13.9 1.0 NA A:HEM154 2.1 12.4 1.0 NE2 A:HIS93 2.2 11.9 1.0 O1 A:NSM155 2.7 14.1 1.0 C4C A:HEM154 3.0 11.1 1.0 C1C A:HEM154 3.0 11.9 1.0 C1D A:HEM154 3.0 14.5 1.0 C1 A:NSM155 3.0 16.2 0.8 C4B A:HEM154 3.1 14.2 1.0 C4A A:HEM154 3.1 12.6 1.0 C1B A:HEM154 3.1 12.5 1.0 CD2 A:HIS93 3.1 10.8 1.0 C4D A:HEM154 3.1 14.3 1.0 C1A A:HEM154 3.2 13.5 1.0 CE1 A:HIS93 3.2 15.2 1.0 CHD A:HEM154 3.3 12.1 1.0 CHC A:HEM154 3.4 12.1 1.0 CHB A:HEM154 3.5 10.8 1.0 CHA A:HEM154 3.5 10.8 1.0 C3C A:HEM154 4.2 16.2 1.0 C2C A:HEM154 4.2 12.8 1.0 C3B A:HEM154 4.3 14.8 1.0 C2D A:HEM154 4.3 12.6 1.0 ND1 A:HIS93 4.3 14.1 1.0 CG A:HIS93 4.3 12.0 1.0 C2B A:HEM154 4.3 13.2 1.0 C3A A:HEM154 4.3 12.6 1.0 C3D A:HEM154 4.4 14.9 1.0 C2A A:HEM154 4.4 12.4 1.0 CG2 A:VAL68 4.6 10.0 1.0 NE2 A:HIS64 4.7 18.1 1.0

D.M.Copeland, A.H.West, G.B.Richter-Addo. Nitrosoalkane and Nitrosoarene Binding to Myoglobin and Heme Models To Be Published.