Iron in PDB 7ffu: Osmium-Bound Human Serum Transferrin

The structure of Osmium-Bound Human Serum Transferrin, PDB code: 7ffu was solved by M.Wang, H.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.85 / 2.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	137.831, 156.729, 107.313, 90, 90, 90
R / Rfree (%)	19.7 / 22.9

The structure of Osmium-Bound Human Serum Transferrin also contains other interesting chemical elements:

Osmium

(Os)

1 atom

The binding sites of Iron atom in the Osmium-Bound Human Serum Transferrin (pdb code 7ffu). 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 Osmium-Bound Human Serum Transferrin, PDB code: 7ffu:

Iron binding site 1 out of 1 in the Osmium-Bound Human Serum Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Osmium-Bound Human Serum Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe701 b:58.3 occ:1.00 OH A:TYR517 2.0 82.4 1.0 O9 A:MLI702 2.1 51.3 1.0 OH A:TYR426 2.1 83.6 1.0 OD1 A:ASP392 2.1 82.2 1.0 O7 A:MLI702 2.1 55.4 1.0 NE2 A:HIS585 2.4 50.8 1.0 C3 A:MLI702 3.1 50.3 1.0 CZ A:TYR426 3.1 66.9 1.0 C2 A:MLI702 3.2 52.3 1.0 CD2 A:HIS585 3.2 51.6 1.0 CG A:ASP392 3.2 65.0 1.0 CZ A:TYR517 3.2 57.5 1.0 CE1 A:HIS585 3.4 52.1 1.0 C1 A:MLI702 3.6 44.3 1.0 O A:HOH804 3.6 78.1 1.0 CB A:ASP392 3.8 47.7 1.0 CE2 A:TYR426 3.8 62.7 1.0 CE1 A:TYR426 4.0 66.3 1.0 CE1 A:TYR517 4.1 55.0 1.0 CE2 A:TYR517 4.1 47.0 1.0 O8 A:MLI702 4.1 56.8 1.0 OD2 A:ASP392 4.2 67.7 1.0 O6 A:MLI702 4.3 52.0 1.0 CB A:THR457 4.3 58.7 1.0 NH1 A:ARG632 4.4 101.0 1.0 CG A:HIS585 4.4 52.3 1.0 ND1 A:HIS585 4.5 51.9 1.0 CA A:ASP392 4.5 55.0 1.0 OG1 A:THR457 4.6 57.6 1.0 N A:THR457 4.7 50.8 1.0 N A:ALA458 4.7 46.6 1.0

M.Wang, H.Wang, X.Xu, T.P.Lai, Y.Zhou, Q.Hao, H.Li, H.Sun. Binding of Ruthenium and Osmium at Non‐Iron Sites of Transferrin Accounts For Their Iron-Independent Cellular Uptake. J.Inorg.Biochem. V. 234 11885 2022.
ISSN: ISSN 0162-0134
PubMed: 35690040
DOI: 10.1016/J.JINORGBIO.2022.111885