Iron in PDB 5hav: Sperm Whale Myoglobin Mutant L29H F33Y F43H (F33Y Cubmb) with Oxygen Bound

The structure of Sperm Whale Myoglobin Mutant L29H F33Y F43H (F33Y Cubmb) with Oxygen Bound, PDB code: 5hav was solved by I.D.Petrik, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.83 / 1.27
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.632, 47.609, 76.534, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 17.8

The binding sites of Iron atom in the Sperm Whale Myoglobin Mutant L29H F33Y F43H (F33Y Cubmb) with Oxygen Bound (pdb code 5hav). 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 Sperm Whale Myoglobin Mutant L29H F33Y F43H (F33Y Cubmb) with Oxygen Bound, PDB code: 5hav:

Iron binding site 1 out of 1 in the Sperm Whale Myoglobin Mutant L29H F33Y F43H (F33Y Cubmb) with Oxygen Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sperm Whale Myoglobin Mutant L29H F33Y F43H (F33Y Cubmb) with Oxygen Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:10.5 occ:1.00 FE A:HEM201 0.0 10.5 1.0 O2 A:OXY202 1.8 10.9 0.4 NA A:HEM201 2.0 10.5 1.0 NC A:HEM201 2.0 11.2 1.0 ND A:HEM201 2.0 11.1 1.0 NB A:HEM201 2.0 10.4 1.0 NE2 A:HIS93 2.1 10.7 1.0 O1 A:OXY202 2.7 14.6 0.4 CE1 A:HIS93 3.0 11.2 1.0 C1A A:HEM201 3.0 10.6 1.0 C4C A:HEM201 3.0 11.5 1.0 C4A A:HEM201 3.1 10.0 1.0 C1C A:HEM201 3.1 11.5 1.0 C1D A:HEM201 3.1 12.2 1.0 C1B A:HEM201 3.1 9.8 1.0 C4D A:HEM201 3.1 11.4 1.0 C4B A:HEM201 3.1 9.7 1.0 CD2 A:HIS93 3.1 11.0 1.0 CHD A:HEM201 3.4 12.1 1.0 CHA A:HEM201 3.4 11.2 1.0 CHC A:HEM201 3.5 10.6 1.0 CHB A:HEM201 3.5 10.0 1.0 ND1 A:HIS93 4.2 11.6 1.0 O A:HOH301 4.2 16.9 0.6 CG A:HIS93 4.3 10.8 1.0 C3C A:HEM201 4.3 12.5 1.0 C2A A:HEM201 4.3 11.4 1.0 C3B A:HEM201 4.3 9.9 1.0 C2D A:HEM201 4.3 12.9 1.0 C2C A:HEM201 4.3 11.3 1.0 C3A A:HEM201 4.3 10.4 1.0 C2B A:HEM201 4.3 10.3 1.0 C3D A:HEM201 4.3 12.6 1.0 CG2 A:VAL68 4.4 12.3 1.0 O A:HOH301 4.4 19.0 0.4 CE1 A:HIS64 4.5 12.9 1.0 NE2 A:HIS64 4.8 13.3 1.0

I.D.Petrik, R.Davydov, M.Ross, X.Zhao, B.Hoffman, Y.Lu. Spectroscopic and Crystallographic Evidence For the Role of A Water-Containing H-Bond Network in Oxidase Activity of An Engineered Myoglobin. J.Am.Chem.Soc. V. 138 1134 2016.
ISSN: ESSN 1520-5126
PubMed: 26716352
DOI: 10.1021/JACS.5B12004