Iron in PDB 5y6k: Human Serum Trnasferrin Bound to A Fluorescent Probe

The structure of Human Serum Trnasferrin Bound to A Fluorescent Probe, PDB code: 5y6k was solved by N.Jiang, T.Cheng, M.Wang, G.C.F.Chan, L.Jin, H.Li, H.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	103.29 / 2.86
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	138.012, 155.752, 107.554, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 23.5

The binding sites of Iron atom in the Human Serum Trnasferrin Bound to A Fluorescent Probe (pdb code 5y6k). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Serum Trnasferrin Bound to A Fluorescent Probe, PDB code: 5y6k:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Serum Trnasferrin Bound to A Fluorescent Probe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Serum Trnasferrin Bound to A Fluorescent Probe within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe702 b:65.1 occ:1.00 O9 A:MLI701 1.8 69.3 1.0 OH A:TYR517 1.9 76.1 1.0 O7 A:MLI701 2.0 67.8 1.0 NE2 A:HIS585 2.2 69.4 1.0 OH A:TYR426 2.3 66.0 1.0 OD1 A:ASP392 2.4 75.0 1.0 C3 A:MLI701 2.9 65.3 1.0 C2 A:MLI701 3.0 65.8 1.0 CD2 A:HIS585 3.1 80.5 1.0 CZ A:TYR517 3.1 51.8 1.0 OG1 A:THR457 3.2 94.5 1.0 CE1 A:HIS585 3.2 69.2 1.0 CG A:ASP392 3.2 56.7 1.0 CZ A:TYR426 3.3 72.9 1.0 C1 A:MLI701 3.4 64.1 1.0 CB A:ASP392 3.8 51.4 1.0 CE2 A:TYR426 3.9 80.4 1.0 CE2 A:TYR517 3.9 41.5 1.0 O8 A:MLI701 4.0 60.5 1.0 CE1 A:TYR517 4.0 47.6 1.0 O6 A:MLI701 4.2 59.7 1.0 OD2 A:ASP392 4.2 57.0 1.0 CE1 A:TYR426 4.3 67.3 1.0 CG A:HIS585 4.3 71.5 1.0 ND1 A:HIS585 4.3 78.1 1.0 CA A:ASP392 4.4 52.2 1.0 CB A:THR457 4.6 83.2 1.0

Iron binding site 2 out of 2 in the Human Serum Trnasferrin Bound to A Fluorescent Probe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Serum Trnasferrin Bound to A Fluorescent Probe within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe703 b:97.0 occ:1.00 N1 A:8R6704 2.0 0.1 1.0 OH A:TYR188 2.1 44.2 1.0 O13 A:8R6704 2.2 0.7 1.0 O5 A:8R6704 2.2 0.6 1.0 C10 A:8R6704 2.2 95.8 1.0 C11 A:8R6704 2.4 83.1 1.0 C3 A:8R6704 2.6 97.5 1.0 C2 A:8R6704 2.6 0.2 1.0 CZ A:TYR188 3.1 66.3 1.0 C6 A:8R6704 3.3 83.8 1.0 CE1 A:TYR188 3.3 69.2 1.0 O12 A:8R6704 3.5 61.1 1.0 O4 A:8R6704 3.6 96.2 1.0 C14 A:8R6704 4.0 64.9 1.0 N A:SER125 4.1 26.8 1.0 CD A:ARG124 4.3 33.1 1.0 O A:HOH801 4.3 43.4 1.0 CE2 A:TYR188 4.4 84.0 1.0 C7 A:8R6704 4.4 0.4 1.0 CB A:ARG124 4.4 26.0 1.0 CE A:LYS206 4.5 0.5 1.0 C15 A:8R6704 4.5 81.0 1.0 CB A:SER125 4.6 43.3 1.0 CG A:ARG124 4.7 29.9 1.0 O9 A:8R6704 4.7 93.5 1.0 N A:ALA126 4.7 32.3 1.0 CD1 A:TYR188 4.7 76.6 1.0 NZ A:LYS206 4.7 0.7 1.0 CA A:SER125 4.8 30.0 1.0 CA A:ARG124 4.8 26.8 1.0 C A:ARG124 4.9 30.2 1.0 NH1 A:ARG124 5.0 60.6 1.0

N.Jiang, T.Cheng, M.Wang, G.C.Chan, L.Jin, H.Li, H.Sun. Tracking Iron-Associated Proteomes in Pathogens By A Fluorescence Approach. Metallomics V. 10 77 2018.
ISSN: ESSN 1756-591X
PubMed: 29323384
DOI: 10.1039/C7MT00275K