Iron in PDB 8f9i: H64A Swmb-Etno Adduct

The structure of H64A Swmb-Etno Adduct, PDB code: 8f9i was solved by V.E.Herrera, L.N.Thomas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.38 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.825, 76.772, 50.529, 90, 103.8, 90
R / Rfree (%)	17.5 / 22.7

The binding sites of Iron atom in the H64A Swmb-Etno Adduct (pdb code 8f9i). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the H64A Swmb-Etno Adduct, PDB code: 8f9i:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the H64A Swmb-Etno Adduct


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of H64A Swmb-Etno Adduct within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:11.4 occ:1.00 FE A:HEM200 0.0 11.4 1.0 ND A:HEM200 1.9 11.5 1.0 N A:NOE201 1.9 20.4 1.0 NA A:HEM200 2.0 11.1 1.0 NE2 A:HIS93 2.0 9.4 1.0 NC A:HEM200 2.1 11.0 1.0 NB A:HEM200 2.1 10.6 1.0 O1 A:NOE201 2.3 28.5 1.0 C1D A:HEM200 2.9 11.7 1.0 C4D A:HEM200 2.9 12.9 1.0 C1A A:HEM200 3.0 11.5 1.0 CE1 A:HIS93 3.0 10.0 1.0 C4B A:HEM200 3.0 10.6 1.0 C4A A:HEM200 3.0 10.6 1.0 C1 A:NOE201 3.0 22.9 1.0 C1B A:HEM200 3.0 10.6 1.0 C4C A:HEM200 3.1 11.0 1.0 CD2 A:HIS93 3.1 9.8 1.0 C1C A:HEM200 3.1 11.8 1.0 CHA A:HEM200 3.4 12.3 1.0 CHD A:HEM200 3.4 10.6 1.0 CHB A:HEM200 3.4 10.7 1.0 CHC A:HEM200 3.5 11.0 1.0 ND1 A:HIS93 4.2 9.9 1.0 C2A A:HEM200 4.2 11.8 1.0 C3A A:HEM200 4.2 11.7 1.0 CG A:HIS93 4.2 9.3 1.0 C2D A:HEM200 4.2 13.2 1.0 C3D A:HEM200 4.2 14.3 1.0 C2B A:HEM200 4.3 10.8 1.0 C3C A:HEM200 4.3 10.6 1.0 C3B A:HEM200 4.3 10.5 1.0 C2C A:HEM200 4.3 10.8 1.0 C2 A:NOE201 4.3 24.2 1.0

Iron binding site 2 out of 2 in the H64A Swmb-Etno Adduct


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of H64A Swmb-Etno Adduct within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:16.2 occ:1.00 FE B:HEM200 0.0 16.2 1.0 N B:NOE201 1.9 15.2 0.6 ND B:HEM200 1.9 17.0 1.0 NA B:HEM200 2.0 15.4 1.0 NE2 B:HIS93 2.0 13.5 1.0 NC B:HEM200 2.0 15.0 1.0 NB B:HEM200 2.1 12.8 1.0 O1 B:NOE201 2.5 17.4 0.6 O B:HOH301 2.5 10.1 0.4 C1D B:HEM200 2.9 18.1 1.0 C4D B:HEM200 2.9 19.2 1.0 C4B B:HEM200 3.0 13.4 1.0 CE1 B:HIS93 3.0 13.2 1.0 C1B B:HEM200 3.0 14.0 1.0 CD2 B:HIS93 3.0 12.4 1.0 C1A B:HEM200 3.0 15.7 1.0 C4C B:HEM200 3.1 16.4 1.0 C4A B:HEM200 3.1 14.5 1.0 C1C B:HEM200 3.1 14.2 1.0 C1 B:NOE201 3.1 15.8 0.6 CHA B:HEM200 3.4 16.9 1.0 CHD B:HEM200 3.4 17.3 1.0 CHC B:HEM200 3.4 13.0 1.0 CHB B:HEM200 3.5 14.8 1.0 ND1 B:HIS93 4.1 13.0 1.0 C2D B:HEM200 4.2 20.9 1.0 CG B:HIS93 4.2 12.3 1.0 C3D B:HEM200 4.2 21.1 1.0 C2 B:NOE201 4.2 15.4 0.6 C2A B:HEM200 4.2 16.7 1.0 C3B B:HEM200 4.3 13.0 1.0 C2B B:HEM200 4.3 13.1 1.0 C3C B:HEM200 4.3 17.0 1.0 C2C B:HEM200 4.3 15.6 1.0 C3A B:HEM200 4.3 15.9 1.0 CD2 B:HIS97 5.0 21.0 1.0

V.E.Herrera, T.P.Charles, T.G.Scott, K.Y.Prather, N.T.Nguyen, C.D.Sohl, L.M.Thomas, G.B.Richter-Addo. Insights Into Nitrosoalkane Binding to Myoglobin Provided By Crystallography of Wild-Type and Distal Pocket Mutant Derivatives. Biochemistry V. 62 1406 2023.
ISSN: ISSN 0006-2960
PubMed: 37011611
DOI: 10.1021/ACS.BIOCHEM.2C00725