Cobalt in PDB 5iqm: Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N

The structure of Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N, PDB code: 5iqm was solved by C.Giese, J.Eras, A.Kern, M.A.Scharer, G.Capitani, R.Glockshuber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.89 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.190, 62.120, 50.640, 90.00, 108.97, 90.00
R / Rfree (%)	15.1 / 18.5

The binding sites of Cobalt atom in the Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N (pdb code 5iqm). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N, PDB code: 5iqm:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in the Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N


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 the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N within 5.0Å range: probe atom residue distance (Å) B Occ G:Co201 b:19.1 occ:0.48 NE2 G:HIS45 1.9 16.7 1.0 O G:HOH465 2.2 30.4 1.0 O A:HOH304 2.3 21.7 1.0 CD2 G:HIS45 2.8 14.4 1.0 CE1 G:HIS45 2.9 14.8 1.0 HD2 G:HIS45 3.0 17.3 1.0 HE1 G:HIS45 3.2 17.8 1.0 O G:HOH455 3.2 25.8 1.0 O G:HOH310 3.3 27.8 1.0 O G:HOH365 3.5 24.4 1.0 O G:LEU27 3.7 15.8 1.0 CG G:HIS45 4.0 13.2 1.0 ND1 G:HIS45 4.0 15.7 1.0 O G:HOH352 4.0 30.1 1.0 HA G:LEU27 4.2 14.6 1.0 C G:LEU27 4.3 13.3 1.0 OD1 A:ASP46 4.3 19.4 0.5 O G:ASP26 4.4 13.0 1.0 O A:HOH449 4.5 26.2 1.0 HA3 G:GLY28 4.5 19.2 1.0 OD2 A:ASP46 4.7 16.5 0.5 OD1 A:ASP46 4.7 16.1 0.5 CA G:LEU27 4.8 12.1 1.0 HB3 G:ALA43 4.9 19.5 1.0 N G:GLY28 5.0 13.9 1.0

Cobalt binding site 2 out of 4 in the Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N within 5.0Å range: probe atom residue distance (Å) B Occ G:Co202 b:13.8 occ:1.00 OD2 G:ASP26 2.0 12.7 1.0 O A:HOH429 2.1 15.5 1.0 O A:HOH424 2.1 14.9 1.0 NE2 A:HIS114 2.2 14.1 1.0 O G:HOH317 2.2 14.1 1.0 O G:HOH444 2.2 14.8 1.0 CG G:ASP26 3.0 14.6 1.0 CD2 A:HIS114 3.1 10.7 1.0 CE1 A:HIS114 3.2 13.7 1.0 HD2 A:HIS114 3.3 12.8 1.0 OD1 G:ASP26 3.3 13.9 1.0 HE1 A:HIS114 3.4 16.4 1.0 HG3 A:PRO116 3.7 20.2 1.0 O G:HOH423 4.0 23.7 1.0 O G:HOH474 4.1 24.5 1.0 O G:HOH467 4.1 32.8 1.0 O A:HOH484 4.1 33.6 1.0 HD3 A:PRO116 4.2 16.7 1.0 O F:HOH109 4.2 18.1 1.0 ND1 A:HIS114 4.3 14.2 1.0 HA2 G:GLY28 4.3 19.2 1.0 HD3 F:ARG8 4.3 18.9 1.0 CG A:HIS114 4.3 10.9 1.0 O A:HOH314 4.3 23.5 1.0 O A:HOH359 4.3 20.1 1.0 O A:HOH343 4.4 17.2 1.0 CB G:ASP26 4.4 12.4 1.0 HB3 A:PRO116 4.5 20.4 1.0 HB2 G:ASP26 4.5 14.9 1.0 HB3 F:ARG8 4.5 15.8 1.0 CG A:PRO116 4.6 16.9 1.0 HB3 G:ASP26 4.7 14.9 1.0 CD A:PRO116 4.9 13.9 1.0 H G:GLY28 4.9 16.7 1.0 HB2 F:ARG8 5.0 15.8 1.0 O A:HOH460 5.0 30.1 1.0

Cobalt binding site 3 out of 4 in the Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N within 5.0Å range: probe atom residue distance (Å) B Occ G:Co203 b:14.1 occ:0.80 O G:HOH430 2.0 17.8 1.0 O A:HOH432 2.1 22.9 1.0 O A:HOH340 2.1 19.3 1.0 OD2 A:ASP26 2.1 15.0 1.0 NE2 G:HIS114 2.2 20.0 1.0 O G:HOH426 2.2 21.9 1.0 CG A:ASP26 3.1 14.6 1.0 CE1 G:HIS114 3.1 20.6 1.0 CD2 G:HIS114 3.2 16.8 1.0 HE1 G:HIS114 3.3 24.7 1.0 HD2 G:HIS114 3.3 20.2 1.0 OD1 A:ASP26 3.4 14.4 1.0 HG3 G:PRO116 3.7 18.5 1.0 O A:HOH406 4.0 24.7 1.0 O B:HOH112 4.2 20.2 1.0 HA2 A:GLY28 4.2 16.1 1.0 ND1 G:HIS114 4.2 16.9 1.0 O B:HOH126 4.3 25.2 1.0 HD3 B:ARG8 4.3 19.2 1.0 CG G:HIS114 4.3 14.0 1.0 O G:HOH381 4.3 28.3 1.0 HD3 G:PRO116 4.4 18.7 1.0 O G:HOH314 4.4 31.8 1.0 HB3 G:PRO116 4.5 20.2 1.0 O G:HOH367 4.5 19.7 1.0 CB A:ASP26 4.5 13.9 1.0 CG G:PRO116 4.6 15.4 1.0 HB2 A:ASP26 4.6 16.6 1.0 HB3 B:ARG8 4.7 15.3 1.0 HB3 A:ASP26 4.8 16.6 1.0 H A:GLY28 5.0 16.4 1.0

Cobalt binding site 4 out of 4 in the Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Crystal Structure of the E. Coli Type 1 Pilus Subunit Fimg (Engineered Variant with Substitution Q134E; N-Terminal Fimg Residues 1-12 Truncated) in Complex with the Donor Strand Peptide DSF_T4R-T6R-D13N within 5.0Å range: probe atom residue distance (Å) B Occ A:Co201 b:17.6 occ:0.46 O A:HOH469 2.0 30.2 1.0 NE2 A:HIS45 2.0 19.0 1.0 O A:HOH422 2.3 32.0 1.0 O A:HOH367 2.3 29.3 1.0 O G:HOH308 2.4 25.3 1.0 O A:HOH302 2.7 36.2 1.0 CD2 A:HIS45 3.0 13.7 1.0 CE1 A:HIS45 3.0 13.5 1.0 HD2 A:HIS45 3.2 16.4 1.0 HE1 A:HIS45 3.2 16.2 1.0 O A:HOH442 3.4 30.1 1.0 O A:LEU27 3.7 14.7 1.0 ND1 A:HIS45 4.1 14.6 1.0 CG A:HIS45 4.1 14.1 1.0 HA A:LEU27 4.2 13.7 1.0 C A:LEU27 4.2 13.9 1.0 HA3 A:GLY28 4.3 16.1 1.0 O A:ASP26 4.4 12.7 1.0 OD1 G:ASP46 4.6 24.2 1.0 O G:HOH305 4.7 41.1 1.0 CA A:LEU27 4.8 11.4 1.0 N A:GLY28 4.9 13.6 1.0

C.Giese, J.Eras, A.Kern, M.A.Scharer, G.Capitani, R.Glockshuber. Accelerating the Association of the Most Stable Protein-Ligand Complex By More Than Two Orders of Magnitude. Angew.Chem.Int.Ed.Engl. V. 55 9350 2016.
ISSN: ESSN 1521-3773
PubMed: 27351462
DOI: 10.1002/ANIE.201603652