Cobalt in PDB 5iqn: 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_SRIRIRGYVR

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_SRIRIRGYVR, PDB code: 5iqn 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)	25.38 / 1.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	25.680, 52.880, 83.140, 90.00, 98.71, 90.00
R / Rfree (%)	11.8 / 14.6

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_SRIRIRGYVR (pdb code 5iqn). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 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_SRIRIRGYVR, PDB code: 5iqn:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 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_SRIRIRGYVR


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_SRIRIRGYVR within 5.0Å range: probe atom residue distance (Å) B Occ A:Co201 b:7.4 occ:0.17 HE1 A:HIS45 1.2 18.1 0.8 HE1 A:HIS45 1.4 8.7 0.2 O G:HOH317 1.6 28.0 0.8 CE1 A:HIS45 1.8 7.2 0.2 CE1 A:HIS45 1.9 15.1 0.8 NE2 A:HIS45 2.0 8.3 0.2 O A:HOH462 2.2 17.7 1.0 O A:HOH313 2.5 23.0 1.0 NE2 A:HIS45 2.6 15.9 0.8 ND1 A:HIS45 3.1 14.9 0.8 ND1 A:HIS45 3.1 10.2 0.2 O A:HOH348 3.3 28.9 1.0 CD2 A:HIS45 3.4 9.4 0.2 HA A:LEU27 3.6 9.4 1.0 O A:HOH346 3.7 14.7 0.8 O A:LEU27 3.7 9.8 1.0 O A:HOH384 3.8 16.3 0.9 CD2 A:HIS45 3.8 13.6 0.8 CG A:HIS45 3.9 9.2 0.2 O A:HOH303 3.9 5.0 0.2 HA2 G:GLY73 4.0 14.2 1.0 HD2 A:HIS45 4.0 11.3 0.2 CG A:HIS45 4.1 12.3 0.8 O G:ASP70 4.1 14.8 1.0 C A:LEU27 4.2 8.5 1.0 O G:HOH302 4.2 11.6 0.5 O A:HOH422 4.2 9.8 0.4 HB3 G:ALA69 4.2 18.4 1.0 O A:ASP26 4.2 8.1 0.4 O G:HOH473 4.3 23.0 0.6 HB2 A:ALA43 4.3 14.0 1.0 O A:ASP26 4.3 10.6 0.6 CA A:LEU27 4.4 7.8 1.0 HA G:SER71 4.6 20.2 1.0 HD2 A:HIS45 4.6 16.4 0.8 HB1 G:ALA69 4.7 18.4 1.0 O G:HOH396 4.7 26.1 1.0 HD23 A:LEU27 4.7 13.9 1.0 H G:GLY73 4.8 14.8 1.0 CA G:GLY73 4.9 11.8 1.0 CB G:ALA69 4.9 15.3 1.0 O A:HOH385 5.0 28.4 0.8

Cobalt binding site 2 out of 2 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_SRIRIRGYVR


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_SRIRIRGYVR within 5.0Å range: probe atom residue distance (Å) B Occ G:Co201 b:19.6 occ:0.35 HE1 G:HIS45 1.7 15.0 0.7 O G:HOH420 2.3 23.7 0.6 CE1 G:HIS45 2.4 12.5 0.7 NE2 G:HIS45 2.5 13.1 0.3 O G:HOH496 2.8 45.3 1.0 NE2 G:HIS45 2.9 10.3 0.7 HE1 G:HIS45 3.2 13.4 0.3 CE1 G:HIS45 3.2 11.2 0.3 O G:HOH329 3.2 13.7 1.0 CD2 G:HIS45 3.6 12.1 0.3 ND1 G:HIS45 3.6 10.4 0.7 O G:LEU27 3.7 10.2 1.0 O G:HOH394 3.8 35.5 1.0 HD2 G:HIS45 3.9 14.6 0.3 HA G:LEU27 3.9 10.0 1.0 O G:ASP26 4.2 9.2 1.0 C G:LEU27 4.2 9.5 1.0 CD2 G:HIS45 4.2 9.1 0.7 ND1 G:HIS45 4.4 10.8 0.3 O G:HOH437 4.5 13.9 0.8 CA G:LEU27 4.6 8.3 1.0 CG G:HIS45 4.6 8.8 0.7 CG G:HIS45 4.6 11.2 0.3 O G:HOH479 4.7 14.8 0.7 HB2 G:ALA43 4.7 14.3 1.0 O G:HOH467 4.7 46.0 1.0 HA3 G:GLY28 4.8 12.4 0.8 HD2 G:HIS45 5.0 10.9 0.7 N G:GLY28 5.0 9.8 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