Iron in PDB 5xkw: Myoglobin Mutant F43Y/F46Y

The structure of Myoglobin Mutant F43Y/F46Y, PDB code: 5xkw was solved by H.Yuan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.01 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.856, 48.459, 78.669, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 19

The binding sites of Iron atom in the Myoglobin Mutant F43Y/F46Y (pdb code 5xkw). 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 Myoglobin Mutant F43Y/F46Y, PDB code: 5xkw:

Iron binding site 1 out of 1 in the Myoglobin Mutant F43Y/F46Y


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Myoglobin Mutant F43Y/F46Y within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:19.5 occ:1.00 FE A:HEM201 0.0 19.5 1.0 ND A:HEM201 1.9 20.3 1.0 NA A:HEM201 2.0 19.5 1.0 NC A:HEM201 2.0 20.2 1.0 NB A:HEM201 2.1 19.1 1.0 NE2 A:HIS93 2.1 18.5 1.0 O A:HOH323 2.1 27.0 1.0 CE1 A:HIS93 3.0 21.7 1.0 C1D A:HEM201 3.0 22.7 1.0 C4D A:HEM201 3.0 21.4 1.0 C4B A:HEM201 3.0 17.5 1.0 C4A A:HEM201 3.1 17.1 1.0 C1A A:HEM201 3.1 17.9 1.0 C4C A:HEM201 3.1 20.6 1.0 C1C A:HEM201 3.1 19.7 1.0 C1B A:HEM201 3.1 16.8 1.0 CD2 A:HIS93 3.2 19.8 1.0 CHC A:HEM201 3.4 17.8 1.0 CHD A:HEM201 3.4 23.7 1.0 CHA A:HEM201 3.4 20.7 1.0 CHB A:HEM201 3.5 18.5 1.0 ND1 A:HIS93 4.2 20.0 1.0 C2A A:HEM201 4.2 19.4 1.0 C3A A:HEM201 4.2 18.0 1.0 C2D A:HEM201 4.2 27.0 1.0 C2B A:HEM201 4.3 17.9 1.0 C3C A:HEM201 4.3 23.1 1.0 C3D A:HEM201 4.3 27.6 1.0 CG A:HIS93 4.3 18.9 1.0 C3B A:HEM201 4.3 18.6 1.0 C2C A:HEM201 4.3 21.5 1.0 NE2 A:HIS64 4.3 25.2 1.0 CG2 A:VAL68 4.7 17.9 1.0 CE1 A:HIS64 4.7 27.0 1.0 OH A:TYR43 4.7 61.9 1.0 CD2 A:HIS97 4.9 25.4 1.0

L.L.Li, H.Yuan, F.Liao, B.He, S.Q.Gao, G.B.Wen, X.Tan, Y.W.Lin. Rational Design of Artificial Dye-Decolorizing Peroxidases Using Myoglobin By Engineering Tyr/Trp in the Heme Center Dalton Trans V. 46 11230 2017.
ISSN: ESSN 1477-9234
PubMed: 28795725
DOI: 10.1039/C7DT02302B