Iron in PDB 1ofk: Recombinant Sperm Whale Myoglobin F43H, H64L Mutant (Met)

The structure of Recombinant Sperm Whale Myoglobin F43H, H64L Mutant (Met), PDB code: 1ofk was solved by E.C.Liong, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.80
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.513, 91.513, 46.061, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 19.5

The binding sites of Iron atom in the Recombinant Sperm Whale Myoglobin F43H, H64L Mutant (Met) (pdb code 1ofk). 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 Recombinant Sperm Whale Myoglobin F43H, H64L Mutant (Met), PDB code: 1ofk:

Iron binding site 1 out of 1 in the Recombinant Sperm Whale Myoglobin F43H, H64L Mutant (Met)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Recombinant Sperm Whale Myoglobin F43H, H64L Mutant (Met) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:15.8 occ:1.00 FE A:HEM154 0.0 15.8 1.0 NA A:HEM154 1.9 15.4 1.0 NC A:HEM154 1.9 14.8 1.0 ND A:HEM154 2.0 16.0 1.0 NB A:HEM154 2.0 14.7 1.0 O A:HOH155 2.1 15.2 0.8 NE2 A:HIS93 2.1 15.8 1.0 C4C A:HEM154 3.0 15.5 1.0 C4A A:HEM154 3.0 15.1 1.0 C1C A:HEM154 3.0 15.1 1.0 C4D A:HEM154 3.0 16.9 1.0 C1A A:HEM154 3.0 16.2 1.0 C1D A:HEM154 3.0 16.3 1.0 C1B A:HEM154 3.0 14.6 1.0 C4B A:HEM154 3.0 14.7 1.0 CD2 A:HIS93 3.1 16.0 1.0 CE1 A:HIS93 3.1 16.3 1.0 CHB A:HEM154 3.4 14.5 1.0 CHD A:HEM154 3.4 15.6 1.0 CHC A:HEM154 3.4 14.5 1.0 CHA A:HEM154 3.4 16.4 1.0 ND1 A:HIS93 4.2 16.0 1.0 CG A:HIS93 4.2 15.8 1.0 C3D A:HEM154 4.2 18.4 1.0 C3A A:HEM154 4.2 15.7 1.0 C2C A:HEM154 4.3 15.2 1.0 C2D A:HEM154 4.3 17.6 1.0 C3C A:HEM154 4.3 16.2 1.0 C2A A:HEM154 4.3 16.5 1.0 C3B A:HEM154 4.3 14.5 1.0 C2B A:HEM154 4.3 14.2 1.0 O A:HOH214 4.3 25.3 1.0 CG2 A:VAL68 4.6 14.1 1.0

T.Matsui, S.Ozaki, E.Liong, G.N.Phillips Jr., Y.Watanabe. Effects of the Location of Distal Histidine in the Reaction of Myoglobin with Hydrogen Peroxide. J.Biol.Chem. V. 274 2838 1999.
ISSN: ISSN 0021-9258
PubMed: 9915818
DOI: 10.1074/JBC.274.5.2838