Iron in PDB 1n7x: Human Serum Transferrin, N-Lobe Y45E Mutant

The structure of Human Serum Transferrin, N-Lobe Y45E Mutant, PDB code: 1n7x was solved by T.E.Adams, A.B.Mason, Q.Y.He, P.J.Halbrooks, S.K.Briggs, V.C.Smith, R.T.Macgillivray, S.J.Everse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.917, 56.570, 135.836, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24.3

The binding sites of Iron atom in the Human Serum Transferrin, N-Lobe Y45E Mutant (pdb code 1n7x). 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, N-Lobe Y45E Mutant, PDB code: 1n7x:

Iron binding site 1 out of 1 in the Human Serum Transferrin, N-Lobe Y45E Mutant


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, N-Lobe Y45E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe339 b:18.4 occ:1.00 OH A:TYR188 2.0 11.0 1.0 OH A:TYR95 2.1 14.6 1.0 NE2 A:HIS249 2.3 14.1 1.0 OD1 A:ASP63 2.3 13.7 1.0 O1 A:CO3338 2.3 3.1 0.4 O1 A:CO3338 2.4 9.1 0.6 O2 A:CO3338 2.6 15.8 0.6 C A:CO3338 2.9 11.1 0.6 CZ A:TYR188 3.0 12.6 1.0 O2 A:CO3338 3.1 9.0 0.4 C A:CO3338 3.1 7.6 0.4 CZ A:TYR95 3.2 15.4 1.0 CD2 A:HIS249 3.2 11.2 1.0 CE1 A:HIS249 3.4 13.4 1.0 CG A:ASP63 3.4 12.4 1.0 CE2 A:TYR95 3.7 14.7 1.0 O A:HOH553 3.8 19.4 0.9 CE2 A:TYR188 3.8 13.6 1.0 CE1 A:TYR188 3.9 12.1 1.0 CB A:ASP63 3.9 13.8 1.0 O3 A:CO3338 4.2 7.9 0.6 CE1 A:TYR95 4.2 15.1 1.0 NZ A:LYS296 4.3 12.1 1.0 O3 A:CO3338 4.3 6.0 0.4 CG A:HIS249 4.4 12.2 1.0 OD2 A:ASP63 4.4 15.5 1.0 ND1 A:HIS249 4.4 13.6 1.0 CB A:SER125 4.5 14.7 1.0 CA A:ASP63 4.5 13.4 1.0 N A:ALA126 4.9 15.6 1.0 OG A:SER125 4.9 17.2 1.0 CD2 A:TYR95 5.0 15.7 1.0 CD A:LYS296 5.0 13.4 1.0

T.E.Adams, A.B.Mason, Q.Y.He, P.J.Halbrooks, S.K.Briggs, V.C.Smith, R.T.Macgillivray, S.J.Everse. The Position of Arginine 124 Controls the Rate of Iron Release From the N-Lobe of Human Serum Transferrin. A Structural Study J.Biol.Chem. V. 278 6027 2003.
ISSN: ISSN 0021-9258
PubMed: 12458193
DOI: 10.1074/JBC.M210349200