Iron in PDB 6jas: Human Serum Transferrin with Iron Citrate Bound

The structure of Human Serum Transferrin with Iron Citrate Bound, PDB code: 6jas was solved by M.Wang, H.Wang, H.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.58 / 2.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	136.567, 157.153, 107.265, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 21.9

The binding sites of Iron atom in the Human Serum Transferrin with Iron Citrate Bound (pdb code 6jas). 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 Transferrin with Iron Citrate Bound, PDB code: 6jas:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Serum Transferrin with Iron Citrate Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Serum Transferrin with Iron Citrate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe701 b:42.2 occ:1.00 O9 A:MLI703 2.0 35.3 1.0 OH A:TYR517 2.0 61.7 1.0 O7 A:MLI703 2.0 38.7 1.0 OD1 A:ASP392 2.2 60.4 1.0 OH A:TYR426 2.3 50.3 1.0 NE2 A:HIS585 2.3 41.9 1.0 C3 A:MLI703 2.9 32.5 1.0 C2 A:MLI703 3.0 36.9 1.0 CZ A:TYR517 3.2 41.2 1.0 CG A:ASP392 3.2 41.7 1.0 CD2 A:HIS585 3.3 45.6 1.0 CE1 A:HIS585 3.3 42.8 1.0 C1 A:MLI703 3.4 19.8 1.0 CZ A:TYR426 3.4 52.5 1.0 CB A:ASP392 3.7 39.6 1.0 O8 A:MLI703 3.9 41.0 1.0 CE1 A:TYR517 4.0 42.4 1.0 CE2 A:TYR517 4.0 41.4 1.0 CE1 A:TYR426 4.1 45.5 1.0 O6 A:MLI703 4.2 42.8 1.0 OD2 A:ASP392 4.2 47.9 1.0 CE2 A:TYR426 4.2 50.6 1.0 CA A:ASP392 4.4 41.8 1.0 ND1 A:HIS585 4.4 44.8 1.0 CB A:THR457 4.4 51.6 1.0 CG A:HIS585 4.5 44.9 1.0 N A:ALA458 4.7 39.9 1.0 N A:THR457 4.8 38.4 1.0 OG1 A:THR457 4.8 56.5 1.0

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


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Serum Transferrin with Iron Citrate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe702 b:51.8 occ:1.00 O6 A:CIT704 1.9 75.5 1.0 O A:HOH870 2.1 51.9 1.0 O A:HOH802 2.2 57.2 1.0 C6 A:CIT704 2.4 92.1 1.0 O5 A:CIT704 2.8 0.1 1.0 O7 A:CIT704 3.3 0.3 1.0 C3 A:CIT704 3.4 97.7 1.0 OG1 A:THR120 3.9 34.5 1.0 CE A:LYS206 4.0 48.2 1.0 NH1 A:ARG124 4.2 34.9 1.0 CG2 A:THR120 4.2 20.2 1.0 CB A:THR120 4.3 31.0 1.0 CD A:ARG124 4.3 36.3 1.0 CB A:ALA126 4.4 18.0 1.0 C2 A:CIT704 4.5 0.5 1.0 C4 A:CIT704 4.5 93.7 1.0 CG A:LYS206 4.5 43.1 1.0 N A:ALA126 4.6 18.1 1.0 CB A:ARG124 4.7 23.2 1.0 CD A:LYS206 4.7 46.3 1.0 N A:GLY127 4.8 20.5 1.0 CB A:TYR188 4.8 48.6 1.0 NZ A:LYS206 4.9 47.3 1.0

M.Wang, H.Wang, H.Sun. Binding of Ruthenium and Osmium at Non-Iron Sites of Transferrin Explains Their Iron-Independent Cellular Uptake To Be Published.