Iron in PDB 1d4n: Human Serum Transferrin

The structure of Human Serum Transferrin, PDB code: 1d4n was solved by H.-W.Yang, R.T.A.Macgillivray, J.Chen, Y.Luo, Y.Wang, G.D.Brayer, A.Mason, R.C.Woodworth, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.030, 57.910, 135.900, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.8

The binding sites of Iron atom in the Human Serum Transferrin (pdb code 1d4n). 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 Human Serum Transferrin, PDB code: 1d4n:

Iron binding site 1 out of 1 in the 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 Human Serum Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe339 b:16.3 occ:1.00 OH A:TYR188 2.0 15.3 1.0 OH A:TYR95 2.1 16.0 1.0 O1 A:CO3338 2.1 13.5 1.0 NE2 A:HIS249 2.2 14.0 1.0 OD1 A:ASP63 2.4 14.9 1.0 O2 A:CO3338 2.6 16.4 1.0 C A:CO3338 2.7 17.2 1.0 CZ A:TYR188 3.0 12.8 1.0 CZ A:TYR95 3.1 17.2 1.0 CE1 A:HIS249 3.1 11.1 1.0 CD2 A:HIS249 3.2 10.2 1.0 CG A:ASP63 3.4 10.6 1.0 CE2 A:TYR95 3.7 13.2 1.0 CB A:ASP63 3.7 9.5 1.0 CE1 A:TYR188 3.8 14.1 1.0 CE2 A:TYR188 3.9 13.5 1.0 O3 A:CO3338 3.9 11.0 1.0 O A:HOH342 3.9 10.5 1.0 CE1 A:TYR95 4.2 14.3 1.0 ND1 A:HIS249 4.3 14.3 1.0 CG A:HIS249 4.3 12.1 1.0 NH2 A:ARG124 4.3 35.2 1.0 NZ A:LYS296 4.4 12.4 1.0 CA A:ASP63 4.4 11.6 1.0 OD2 A:ASP63 4.5 13.6 1.0 CB A:SER125 4.6 13.2 1.0 N A:ALA126 4.9 13.8 1.0 NE A:ARG124 4.9 33.6 1.0 CD A:LYS296 4.9 13.8 1.0 N A:SER125 5.0 12.8 1.0 CD2 A:TYR95 5.0 14.3 1.0 CZ A:ARG124 5.0 38.4 1.0 OG A:SER125 5.0 13.4 1.0

A.H.Yang, R.T.Macgillivray, J.Chen, Y.Luo, Y.Wang, G.D.Brayer, A.B.Mason, R.C.Woodworth, M.E.Murphy. Crystal Structures of Two Mutants (K206Q, H207E) of the N-Lobe of Human Transferrin with Increased Affinity For Iron. Protein Sci. V. 9 49 2000.
ISSN: ISSN 0961-8368
PubMed: 10739246