Cobalt in PDB 3bfq: 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: 3bfq 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)	15.00 / 1.34
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.050, 24.500, 54.150, 90.00, 113.77, 90.00
R / Rfree (%)	13.2 / 17.9

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

Cobalt 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 Cobalt with other atoms in the Co 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 G:Co1 b:14.9 occ:0.61 O G:HOH284 1.8 20.0 1.0 O G:HOH286 2.0 31.2 1.0 NE2 G:HIS45 2.1 17.0 1.0 O G:HOH285 2.1 19.5 1.0 O G:HOH254 2.1 23.0 1.0 O G:HOH253 2.2 25.0 1.0 CE1 G:HIS45 3.0 18.0 1.0 CD2 G:HIS45 3.2 14.9 1.0 O G:LEU27 4.1 15.4 1.0 ND1 G:HIS45 4.1 16.1 1.0 O G:ASP26 4.1 12.8 1.0 O G:HOH198 4.2 23.5 1.0 O G:HOH225 4.2 17.5 0.5 CG G:HIS45 4.3 14.0 1.0 C G:LEU27 4.5 14.1 1.0 O G:HOH158 4.6 18.0 1.0 O G:HOH287 4.6 38.7 1.0 CA G:LEU27 4.7 11.9 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