Yttrium in PDB 3bfw: Crystal Structure of Truncated Fimg (Fimgt) in Complex with the Donor Strand Peptide of Fimf (Dsf)

The structure of Crystal Structure of Truncated Fimg (Fimgt) in Complex with the Donor Strand Peptide of Fimf (Dsf), PDB code: 3bfw was solved by O.Eidam, G.Capitani, M.G.Grutter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	24.610, 46.740, 48.620, 92.82, 90.92, 92.51
R / Rfree (%)	20.4 / 23.8

The binding sites of Yttrium atom in the Crystal Structure of Truncated Fimg (Fimgt) in Complex with the Donor Strand Peptide of Fimf (Dsf) (pdb code 3bfw). This binding sites where shown within 5.0 Angstroms radius around Yttrium atom.
In total only one binding site of Yttrium was determined in the Crystal Structure of Truncated Fimg (Fimgt) in Complex with the Donor Strand Peptide of Fimf (Dsf), PDB code: 3bfw:

Yttrium binding site 1 out of 1 in the Crystal Structure of Truncated Fimg (Fimgt) in Complex with the Donor Strand Peptide of Fimf (Dsf)


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 1 of Crystal Structure of Truncated Fimg (Fimgt) in Complex with the Donor Strand Peptide of Fimf (Dsf) within 5.0Å range: probe atom residue distance (Å) B Occ A:Y1 b:6.6 occ:0.70 OD1 A:ASP46 2.3 14.4 1.0 OE1 A:GLN118 2.3 15.5 1.0 O A:HOH168 2.3 20.6 1.0 O A:HOH147 2.5 9.2 1.0 OD1 A:ASP91 2.5 9.2 1.0 OD2 A:ASP91 2.6 12.4 1.0 CG A:ASP91 2.9 10.0 1.0 CD A:GLN118 3.3 16.1 1.0 CG A:ASP46 3.5 17.2 1.0 CG A:GLN118 3.9 15.8 1.0 O A:LEU117 4.2 6.4 1.0 NE2 A:GLN118 4.3 17.8 1.0 OD2 A:ASP46 4.3 17.8 1.0 CB A:ASP91 4.4 11.7 1.0 CB A:ASP46 4.5 12.2 1.0 O A:HOH259 4.6 17.2 1.0 CA A:ASP46 4.8 11.5 1.0 C A:LEU117 4.9 6.8 1.0 O A:HOH194 5.0 16.5 1.0

C.Puorger, O.Eidam, G.Capitani, D.Erilov, M.G.Grutter, R.Glockshuber. Infinite Kinetic Stability Against Dissociation of Supramolecular Protein Complexes Through Donor Strand Complementation Structure V. 16 631 2008.
ISSN: ISSN 0969-2126
PubMed: 18400183
DOI: 10.1016/J.STR.2008.01.013