Iron in PDB 5eil: Computational Design of A High-Affinity Metalloprotein Homotrimer Containing A Metal Chelating Non-Canonical Amino Acid

The structure of Computational Design of A High-Affinity Metalloprotein Homotrimer Containing A Metal Chelating Non-Canonical Amino Acid, PDB code: 5eil was solved by B.Sankaran, P.H.Zwart, J.H.Mills, J.H.Pereira, D.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.92 / 2.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.107, 63.940, 64.831, 90.00, 116.87, 90.00
R / Rfree (%)	21.4 / 24.5

The binding sites of Iron atom in the Computational Design of A High-Affinity Metalloprotein Homotrimer Containing A Metal Chelating Non-Canonical Amino Acid (pdb code 5eil). 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 Computational Design of A High-Affinity Metalloprotein Homotrimer Containing A Metal Chelating Non-Canonical Amino Acid, PDB code: 5eil:

Iron binding site 1 out of 1 in the Computational Design of A High-Affinity Metalloprotein Homotrimer Containing A Metal Chelating Non-Canonical Amino Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Computational Design of A High-Affinity Metalloprotein Homotrimer Containing A Metal Chelating Non-Canonical Amino Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:31.0 occ:1.00 N2 B:BP59 2.0 41.0 1.0 N2 A:BP59 2.0 53.2 1.0 N2 C:BP59 2.0 38.7 1.0 N1 C:BP59 2.1 41.3 1.0 N1 A:BP59 2.1 56.6 1.0 N1 B:BP59 2.1 47.0 1.0 C6 B:BP59 2.8 43.2 1.0 C6 C:BP59 2.8 39.9 1.0 C6 A:BP59 2.8 54.6 1.0 C3 C:BP59 2.8 41.4 1.0 C3 B:BP59 2.8 46.7 1.0 C3 A:BP59 2.8 56.4 1.0 C11 B:BP59 3.1 38.5 1.0 C11 A:BP59 3.1 50.7 1.0 C11 C:BP59 3.1 37.2 1.0 H11 B:BP59 3.1 46.2 1.0 H11 A:BP59 3.2 60.9 1.0 H11 C:BP59 3.2 44.6 1.0 C4 C:BP59 3.2 42.1 1.0 C4 B:BP59 3.2 50.0 1.0 C4 A:BP59 3.2 57.6 1.0 H4 C:BP59 3.4 50.5 1.0 H4 A:BP59 3.4 69.1 1.0 H4 B:BP59 3.4 60.0 1.0 C7 B:BP59 4.1 42.7 1.0 C7 C:BP59 4.1 39.6 1.0 C7 A:BP59 4.2 54.0 1.0 C2 C:BP59 4.2 42.9 1.0 C2 B:BP59 4.2 49.6 1.0 C2 A:BP59 4.2 57.4 1.0 C9 B:BP59 4.3 37.8 1.0 C9 C:BP59 4.4 36.6 1.0 C9 A:BP59 4.4 49.7 1.0 C5 C:BP59 4.5 43.4 1.0 C5 B:BP59 4.5 52.5 1.0 C5 A:BP59 4.5 59.0 1.0 HG3 B:GLU5 4.6 61.6 1.0 C8 B:BP59 4.7 39.9 1.0 C8 C:BP59 4.8 38.1 1.0 C8 A:BP59 4.8 52.2 1.0 H7 B:BP59 4.8 51.2 1.0 H7 C:BP59 4.8 47.5 1.0 H2 B:BP59 4.8 59.6 1.0 H2 C:BP59 4.8 51.5 1.0 H7 A:BP59 4.8 64.8 1.0 C1 C:BP59 4.8 43.8 1.0 C1 B:BP59 4.9 51.9 1.0 H2 A:BP59 4.9 68.9 1.0 HG2 C:GLU5 4.9 55.9 0.5 C1 A:BP59 4.9 58.8 1.0

J.H.Mills, W.Sheffler, M.E.Ener, P.J.Almhjell, G.Oberdorfer, J.H.Pereira, F.Parmeggiani, B.Sankaran, P.H.Zwart, D.Baker. Computational Design of A Homotrimeric Metalloprotein with A Trisbipyridyl Core. Proc. Natl. Acad. Sci. V. 113 15012 2016U.S.A..
ISSN: ESSN 1091-6490
PubMed: 27940918
DOI: 10.1073/PNAS.1600188113