Iron in PDB 3mgu: Structure of S. Cerevisiae TPA1 Protein, A Proline Hydroxylase Modifying Ribosomal Protein RPS23

The structure of Structure of S. Cerevisiae TPA1 Protein, A Proline Hydroxylase Modifying Ribosomal Protein RPS23, PDB code: 3mgu was solved by J.Henri, D.Rispal, E.Bayart, H.Van Tilbeurgh, B.Seraphin, M.Graille, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.92 / 2.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.180, 104.840, 205.570, 90.00, 90.00, 90.00
R / Rfree (%)	23.9 / 29.6

The binding sites of Iron atom in the Structure of S. Cerevisiae TPA1 Protein, A Proline Hydroxylase Modifying Ribosomal Protein RPS23 (pdb code 3mgu). 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 Structure of S. Cerevisiae TPA1 Protein, A Proline Hydroxylase Modifying Ribosomal Protein RPS23, PDB code: 3mgu:

Iron binding site 1 out of 1 in the Structure of S. Cerevisiae TPA1 Protein, A Proline Hydroxylase Modifying Ribosomal Protein RPS23


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of S. Cerevisiae TPA1 Protein, A Proline Hydroxylase Modifying Ribosomal Protein RPS23 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1501 b:67.6 occ:1.00 NE2 A:HIS227 2.3 51.1 1.0 OD1 A:ASP161 2.4 57.4 1.0 NE2 A:HIS159 2.6 55.1 1.0 OD2 A:ASP161 2.7 67.3 1.0 CG A:ASP161 2.8 63.1 1.0 CD2 A:HIS227 3.0 50.7 1.0 CE1 A:HIS159 3.1 50.6 1.0 O A:HOH667 3.2 59.5 1.0 O A:HOH645 3.4 71.5 1.0 CE1 A:HIS227 3.5 54.3 1.0 CD2 A:HIS159 3.8 54.0 1.0 CB A:ASP161 4.3 56.5 1.0 CG A:HIS227 4.3 49.0 1.0 ND1 A:HIS159 4.3 53.2 1.0 CD1 A:LEU156 4.4 57.1 1.0 ND1 A:HIS227 4.5 52.7 1.0 CG A:HIS159 4.7 55.9 1.0 NE2 A:GLN242 4.7 79.1 1.0 CZ2 A:TRP244 4.8 78.4 1.0 CA A:ASP161 5.0 64.7 1.0

J.Henri, D.Rispal, E.Bayart, H.Van Tilbeurgh, B.Seraphin, M.Graille. Structural and Functional Insights Into S. Cerevisiae TPA1, A Putative Prolyl Hydroxylase Influencing Translation Termination and Transcription To Be Published.