Iron in PDB 8f9h: H64A Swmb-Meno Adduct

The structure of H64A Swmb-Meno Adduct, PDB code: 8f9h was solved by V.E.Herrera, L.M.Thomas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.856, 29.027, 64.263, 90, 105.89, 90
R / Rfree (%)	15.2 / 20.1

The binding sites of Iron atom in the H64A Swmb-Meno Adduct (pdb code 8f9h). 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 H64A Swmb-Meno Adduct, PDB code: 8f9h:

Iron binding site 1 out of 1 in the H64A Swmb-Meno 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-Meno Adduct within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:13.7 occ:1.00 FE A:HEM200 0.0 13.7 1.0 ND A:HEM200 1.9 11.9 1.0 N A:NSM201 1.9 14.6 1.0 NA A:HEM200 2.0 12.4 1.0 NB A:HEM200 2.1 13.3 1.0 NE2 A:HIS93 2.1 11.3 1.0 NC A:HEM200 2.1 12.8 1.0 O1 A:NSM201 2.8 17.9 1.0 C1D A:HEM200 2.9 14.0 1.0 C4D A:HEM200 3.0 13.0 1.0 C1 A:NSM201 3.0 16.7 1.0 C4B A:HEM200 3.0 13.9 1.0 C1A A:HEM200 3.0 12.5 1.0 C4A A:HEM200 3.0 12.1 1.0 C1B A:HEM200 3.0 12.7 1.0 CE1 A:HIS93 3.1 12.3 1.0 C4C A:HEM200 3.1 13.6 1.0 C1C A:HEM200 3.1 13.0 1.0 CD2 A:HIS93 3.1 11.5 1.0 CHD A:HEM200 3.4 13.7 1.0 CHB A:HEM200 3.4 12.3 1.0 CHC A:HEM200 3.4 13.3 1.0 CHA A:HEM200 3.4 12.3 1.0 ND1 A:HIS93 4.2 11.1 1.0 C2D A:HEM200 4.2 14.8 1.0 C3D A:HEM200 4.2 14.0 1.0 C2A A:HEM200 4.2 12.2 1.0 C3A A:HEM200 4.2 13.5 1.0 CG A:HIS93 4.2 11.5 1.0 C2B A:HEM200 4.3 13.4 1.0 C3B A:HEM200 4.3 14.0 1.0 C2C A:HEM200 4.3 13.6 1.0 C3C A:HEM200 4.3 13.1 1.0 CG2 A:VAL68 4.7 17.4 1.0 O A:HOH319 4.8 26.0 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