Iron in PDB 5ile: H64A Sperm Whale Myoglobin with A Fe-Tolyl Moiety

The structure of H64A Sperm Whale Myoglobin with A Fe-Tolyl Moiety, PDB code: 5ile was solved by B.Wang, L.M.Thomas, G.B.Richter-Addo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.26 / 1.77
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	90.794, 90.794, 45.317, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 17.9

The binding sites of Iron atom in the H64A Sperm Whale Myoglobin with A Fe-Tolyl Moiety (pdb code 5ile). 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 H64A Sperm Whale Myoglobin with A Fe-Tolyl Moiety, PDB code: 5ile:

Iron binding site 1 out of 1 in the H64A Sperm Whale Myoglobin with A Fe-Tolyl Moiety


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of H64A Sperm Whale Myoglobin with A Fe-Tolyl Moiety within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:19.8 occ:1.00 FE A:6CQ201 0.0 19.8 1.0 C1 A:6CQ201 1.9 20.4 1.0 ND A:6CQ201 2.0 20.4 1.0 NB A:6CQ201 2.1 15.8 1.0 NC A:6CQ201 2.1 17.5 1.0 NA A:6CQ201 2.1 18.3 1.0 NE2 A:HIS93 2.2 19.3 1.0 C2 A:6CQ201 2.9 22.9 1.0 C6 A:6CQ201 2.9 24.5 1.0 C4C A:6CQ201 3.0 19.2 1.0 C1C A:6CQ201 3.0 17.9 1.0 C4D A:6CQ201 3.0 20.1 1.0 C1D A:6CQ201 3.0 19.4 1.0 C1B A:6CQ201 3.1 17.7 1.0 C1A A:6CQ201 3.1 21.1 1.0 C4A A:6CQ201 3.1 19.4 1.0 C4B A:6CQ201 3.1 17.1 1.0 CE1 A:HIS93 3.1 21.8 1.0 CD2 A:HIS93 3.3 18.9 1.0 CHC A:6CQ201 3.5 18.5 1.0 CHA A:6CQ201 3.5 20.9 1.0 CHB A:6CQ201 3.5 18.1 1.0 CHD A:6CQ201 3.5 17.9 1.0 C3 A:6CQ201 4.2 21.9 1.0 C5 A:6CQ201 4.2 25.6 1.0 C3C A:6CQ201 4.3 18.2 1.0 C2D A:6CQ201 4.3 20.6 1.0 C3D A:6CQ201 4.3 22.2 1.0 ND1 A:HIS93 4.3 21.1 1.0 C2C A:6CQ201 4.3 16.7 1.0 C2B A:6CQ201 4.3 17.4 1.0 C2A A:6CQ201 4.3 23.9 1.0 C3B A:6CQ201 4.3 18.1 1.0 C3A A:6CQ201 4.4 20.6 1.0 CG A:HIS93 4.4 19.7 1.0 C4 A:6CQ201 4.7 19.6 1.0

B.Wang, L.M.Thomas, G.B.Richter-Addo. Organometallic Myoglobins: Formation of Fe-Carbon Bonds and Distal Pocket Effects on Aryl Ligand Conformations. J. Inorg. Biochem. V. 164 1 2016.
ISSN: ISSN 1873-3344
PubMed: 27687333
DOI: 10.1016/J.JINORGBIO.2016.06.028