Iron in PDB 3qyt: Diferric Bound Human Serum Transferrin

The structure of Diferric Bound Human Serum Transferrin, PDB code: 3qyt was solved by N.Yang, H.Zhang, M.Wang, Q.Hao, H.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.07 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.845, 90.435, 112.299, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 27.5

The binding sites of Iron atom in the Diferric Bound Human Serum Transferrin (pdb code 3qyt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Diferric Bound Human Serum Transferrin, PDB code: 3qyt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Diferric 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 Diferric Bound Human Serum Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe680 b:30.3 occ:1.00 OH A:TYR426 1.9 38.2 1.0 OH A:TYR517 1.9 27.8 1.0 O3 A:CO3681 2.1 26.7 1.0 OD1 A:ASP392 2.1 41.3 1.0 NE2 A:HIS585 2.1 30.3 1.0 O2 A:CO3681 2.4 22.3 1.0 C A:CO3681 2.6 24.8 1.0 CZ A:TYR426 3.0 37.6 1.0 CD2 A:HIS585 3.1 33.7 1.0 CE1 A:HIS585 3.1 34.0 1.0 CZ A:TYR517 3.2 28.2 1.0 CG A:ASP392 3.3 38.2 1.0 CE2 A:TYR426 3.5 37.8 1.0 O A:HOH687 3.7 14.5 1.0 CE1 A:TYR517 3.8 27.4 1.0 O1 A:CO3681 3.9 22.3 1.0 CE1 A:TYR426 4.0 36.0 1.0 CB A:ASP392 4.1 35.3 1.0 CE2 A:TYR517 4.2 26.1 1.0 ND1 A:HIS585 4.2 30.7 1.0 CG A:HIS585 4.2 33.2 1.0 OD2 A:ASP392 4.2 36.9 1.0 NH2 A:ARG456 4.4 24.7 1.0 CB A:THR457 4.5 32.4 1.0 CA A:ASP392 4.5 32.1 1.0 OG1 A:THR457 4.6 31.4 1.0 NH1 A:ARG632 4.6 41.8 1.0 NE A:ARG456 4.7 23.9 1.0 N A:THR457 4.8 36.8 1.0 N A:ALA458 4.8 30.3 1.0 CD2 A:TYR426 4.8 40.2 1.0

Iron binding site 2 out of 2 in the Diferric Bound Human Serum Transferrin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Diferric Bound Human Serum Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe682 b:60.3 occ:1.00 OH A:TYR188 1.9 74.2 1.0 O1 A:SO4686 1.9 0.1 1.0 OH A:TYR95 2.0 47.8 1.0 O3 A:CO3683 2.3 58.5 1.0 O3 A:SO4686 2.4 0.5 1.0 S A:SO4686 2.4 0.4 1.0 O2 A:CO3683 2.6 51.1 1.0 C A:CO3683 2.8 55.0 1.0 CZ A:TYR95 2.8 46.4 1.0 O2 A:SO4686 2.9 0.5 1.0 CZ A:TYR188 3.1 72.4 1.0 CE1 A:TYR95 3.3 48.1 1.0 CE2 A:TYR95 3.8 47.2 1.0 O4 A:SO4686 3.8 0.7 1.0 CE2 A:TYR188 3.8 66.1 1.0 CE1 A:TYR188 4.1 77.4 1.0 O1 A:CO3683 4.1 53.1 1.0 CB A:SER125 4.2 60.4 1.0 NE A:ARG124 4.4 85.8 1.0 N A:SER125 4.4 58.0 1.0 CD1 A:TYR95 4.5 49.4 1.0 NH2 A:ARG124 4.5 90.9 1.0 OG A:SER125 4.7 65.9 1.0 CA A:SER125 4.9 55.2 1.0 N A:ALA126 4.9 51.5 1.0 CZ A:ARG124 4.9 90.9 1.0 CD2 A:TYR95 4.9 46.3 1.0

N.Yang, H.Zhang, M.Wang, Q.Hao, H.Sun. Iron and Bismuth Bound Human Serum Transferrin Reveals A Partially-Opened Conformation in the N-Lobe Sci Rep V. 2 999 2012.
ISSN: ESSN 2045-2322
PubMed: 23256035
DOI: 10.1038/SREP00999