Iron in PDB 1ryo: Human Serum Transferrin, N-Lobe Bound with Oxalate

The structure of Human Serum Transferrin, N-Lobe Bound with Oxalate, PDB code: 1ryo was solved by P.J.Halbrooks, A.B.Mason, T.E.Adams, S.K.Briggs, S.J.Everse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.092, 57.252, 135.988, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 23.5

The binding sites of Iron atom in the Human Serum Transferrin, N-Lobe Bound with Oxalate (pdb code 1ryo). 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 Bound with Oxalate, PDB code: 1ryo:

Iron binding site 1 out of 1 in the Human Serum Transferrin, N-Lobe Bound with Oxalate


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 Bound with Oxalate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe329 b:5.1 occ:1.00 O1 A:OXL328 2.0 6.6 1.0 OH A:TYR188 2.1 4.4 1.0 NE2 A:HIS249 2.1 5.3 1.0 OH A:TYR95 2.1 3.7 1.0 O2 A:OXL328 2.2 3.8 1.0 OD1 A:ASP63 2.2 4.0 1.0 C1 A:OXL328 2.8 4.5 1.0 C2 A:OXL328 2.9 4.2 1.0 CE1 A:HIS249 3.0 4.2 1.0 CZ A:TYR188 3.1 4.4 1.0 CZ A:TYR95 3.2 4.2 1.0 CD2 A:HIS249 3.2 4.2 1.0 CG A:ASP63 3.2 4.1 1.0 CB A:ASP63 3.7 4.4 1.0 CE2 A:TYR95 3.8 4.8 1.0 CE1 A:TYR188 3.8 4.3 1.0 CE2 A:TYR188 3.9 4.5 1.0 O A:HOH826 4.0 9.9 1.0 O3 A:OXL328 4.0 5.8 1.0 ND1 A:HIS249 4.1 4.2 1.0 CE1 A:TYR95 4.2 4.7 1.0 O4 A:OXL328 4.2 4.8 1.0 CG A:HIS249 4.3 4.4 1.0 NZ A:LYS296 4.3 7.0 1.0 CA A:ASP63 4.3 4.2 1.0 OD2 A:ASP63 4.3 4.7 1.0 O A:HOH399 4.5 8.6 1.0 CB A:SER125 4.6 4.2 1.0 CD A:LYS296 4.8 4.9 1.0 N A:SER125 5.0 5.0 1.0 OG A:SER125 5.0 5.8 1.0 N A:ALA126 5.0 4.7 1.0

P.J.Halbrooks, A.B.Mason, T.E.Adams, S.K.Briggs, S.J.Everse. The Oxalate Effect on Release of Iron From Human Serum Transferrin Explained. J.Mol.Biol. V. 339 217 2004.
ISSN: ISSN 0022-2836
PubMed: 15123433
DOI: 10.1016/J.JMB.2004.03.049