Iron in PDB 1a8e: Human Serum Transferrin, Recombinant N-Terminal Lobe

The structure of Human Serum Transferrin, Recombinant N-Terminal Lobe, PDB code: 1a8e was solved by R.T.A.Macgillivray, S.A.Moore, J.Chen, B.F.Anderson, H.Baker, Y.Luo, M.Bewley, C.A.Smith, M.E.P.Murphy, Y.Wang, A.B.Mason, R.C.Woodworth, G.D.Brayer, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.120, 57.910, 135.640, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / n/a

The binding sites of Iron atom in the Human Serum Transferrin, Recombinant N-Terminal Lobe (pdb code 1a8e). 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, Recombinant N-Terminal Lobe, PDB code: 1a8e:

Iron binding site 1 out of 1 in the Human Serum Transferrin, Recombinant N-Terminal Lobe


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, Recombinant N-Terminal Lobe within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe339 b:20.4 occ:1.00 OH A:TYR188 1.8 18.2 1.0 OH A:TYR95 2.0 20.6 1.0 O2 A:CO3338 2.0 10.5 0.3 OD1 A:ASP63 2.0 19.1 1.0 NE2 A:HIS249 2.0 22.0 1.0 O1 A:CO3338 2.1 13.4 0.7 O2 A:CO3338 2.2 28.7 0.7 O1 A:CO3338 2.4 20.1 0.3 C A:CO3338 2.5 19.4 0.7 C A:CO3338 2.5 19.9 0.3 CZ A:TYR188 2.9 25.2 1.0 CE1 A:HIS249 2.9 21.4 1.0 CZ A:TYR95 3.1 27.2 1.0 CD2 A:HIS249 3.1 22.1 1.0 CG A:ASP63 3.2 21.6 1.0 CE2 A:TYR95 3.6 21.5 1.0 CE1 A:TYR188 3.7 21.8 1.0 CB A:ASP63 3.7 18.7 1.0 CE2 A:TYR188 3.8 22.8 1.0 O3 A:CO3338 3.8 15.8 0.3 O3 A:CO3338 3.8 8.9 0.7 O A:HOH342 3.8 21.1 1.0 ND1 A:HIS249 4.1 21.7 1.0 CE1 A:TYR95 4.1 25.3 1.0 OD2 A:ASP63 4.2 22.2 1.0 CG A:HIS249 4.2 21.6 1.0 NZ A:LYS296 4.3 23.7 1.0 NH2 A:ARG124 4.3 38.3 0.7 CA A:ASP63 4.5 17.7 1.0 CB A:SER125 4.7 19.0 1.0 NE A:ARG124 4.9 46.0 0.7 N A:ALA126 4.9 20.1 1.0 CD A:LYS296 4.9 24.9 1.0 CD2 A:TYR95 4.9 21.9 1.0 N A:SER125 5.0 19.6 1.0 CD1 A:TYR188 5.0 22.4 1.0 OG A:SER125 5.0 21.4 1.0

R.T.Macgillivray, S.A.Moore, J.Chen, B.F.Anderson, H.Baker, Y.Luo, M.Bewley, C.A.Smith, M.E.Murphy, Y.Wang, A.B.Mason, R.C.Woodworth, G.D.Brayer, E.N.Baker. Two High-Resolution Crystal Structures of the Recombinant N-Lobe of Human Transferrin Reveal A Structural Change Implicated in Iron Release. Biochemistry V. 37 7919 1998.
ISSN: ISSN 0006-2960
PubMed: 9609685
DOI: 10.1021/BI980355J