Iron in PDB 4tyx: Structure of Aquoferric Sperm Whale Myoglobin L29H/F33Y/F43H/S92A Mutant

The structure of Structure of Aquoferric Sperm Whale Myoglobin L29H/F33Y/F43H/S92A Mutant, PDB code: 4tyx was solved by A.Bhagi-Damodaran, I.D.Petrik, H.Robinson, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.66 / 1.64
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.467, 47.910, 76.854, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 19.8

The binding sites of Iron atom in the Structure of Aquoferric Sperm Whale Myoglobin L29H/F33Y/F43H/S92A Mutant (pdb code 4tyx). 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 Structure of Aquoferric Sperm Whale Myoglobin L29H/F33Y/F43H/S92A Mutant, PDB code: 4tyx:

Iron binding site 1 out of 1 in the Structure of Aquoferric Sperm Whale Myoglobin L29H/F33Y/F43H/S92A Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Aquoferric Sperm Whale Myoglobin L29H/F33Y/F43H/S92A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:17.2 occ:1.00 FE A:HEM201 0.0 17.2 1.0 NA A:HEM201 2.1 17.9 1.0 ND A:HEM201 2.1 15.8 1.0 O A:HOH408 2.1 20.6 1.0 NC A:HEM201 2.1 16.7 1.0 NE2 A:HIS93 2.2 18.3 1.0 NB A:HEM201 2.2 19.5 1.0 C1A A:HEM201 3.0 19.2 1.0 C4D A:HEM201 3.0 17.9 1.0 C4C A:HEM201 3.1 16.9 1.0 C1D A:HEM201 3.1 18.7 1.0 C4A A:HEM201 3.1 17.1 1.0 C1C A:HEM201 3.1 15.2 1.0 CE1 A:HIS93 3.1 21.7 1.0 C4B A:HEM201 3.1 13.4 1.0 CD2 A:HIS93 3.2 20.4 1.0 C1B A:HEM201 3.2 17.8 1.0 CHA A:HEM201 3.4 21.0 1.0 CHC A:HEM201 3.5 16.6 1.0 CHD A:HEM201 3.5 21.6 1.0 CHB A:HEM201 3.5 17.1 1.0 O A:HOH426 3.9 26.9 1.0 C3D A:HEM201 4.2 24.7 1.0 C2A A:HEM201 4.2 22.8 1.0 C3A A:HEM201 4.2 18.0 1.0 C3C A:HEM201 4.2 17.2 1.0 C2D A:HEM201 4.3 26.4 1.0 ND1 A:HIS93 4.3 20.0 1.0 C2C A:HEM201 4.3 15.8 1.0 CG A:HIS93 4.3 16.7 1.0 C3B A:HEM201 4.4 15.8 1.0 C2B A:HEM201 4.4 15.0 1.0 NE2 A:HIS64 4.5 23.9 1.0 CG2 A:VAL68 4.5 15.3 1.0 CE1 A:HIS64 4.6 22.5 1.0

A.Bhagi-Damodaran, I.D.Petrik, N.M.Marshall, H.Robinson, Y.Lu. Systematic Tuning of Heme Redox Potentials and Its Effects on O2 Reduction Rates in A Designed Oxidase in Myoglobin. J.Am.Chem.Soc. V. 136 11882 2014.
ISSN: ESSN 1520-5126
PubMed: 25076049
DOI: 10.1021/JA5054863