Mercury in PDB 4mty: Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex.

All present enzymatic activity of Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex.:
4.2.1.1;

The structure of Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex., PDB code: 4mty was solved by T.Ogayone, J.Buratto, B.Langlois D'estaintot, M.Stupfel, T.Granier, B.Gallois, Y.Huc, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.85 / 1.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.444, 41.559, 72.064, 90.00, 104.41, 90.00
R / Rfree (%)	10.5 / 12.3

The structure of Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex. also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Mercury atom in the Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex. (pdb code 4mty). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex., PDB code: 4mty:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg304 b:5.9 occ:0.50 HG A:HGB304 0.0 5.9 0.5 HG A:HG309 1.3 5.9 0.3 C7 A:HGB304 2.1 6.7 0.5 SG A:CYS205 2.3 5.8 0.5 O A:GLN136 2.9 7.2 1.0 O A:HOH531 2.9 15.2 1.0 C5 A:HGB304 3.0 9.4 0.5 O A:GLU204 3.1 7.5 1.0 C6 A:HGB304 3.1 10.1 0.5 CB A:CYS205 3.2 5.4 0.5 SG A:CYS205 3.3 5.9 0.3 C A:GLN136 3.3 6.9 1.0 C A:GLU204 3.4 5.5 1.0 CA A:CYS205 3.5 5.3 0.5 CA A:CYS205 3.5 5.5 0.5 N A:CYS205 3.6 5.5 0.5 O A:HOH445 3.7 13.4 1.0 N A:GLN136 3.7 7.7 1.0 N A:CYS205 3.7 4.7 0.5 CB A:CYS205 3.8 6.1 0.5 N A:PRO137 3.9 7.2 1.0 CA A:PRO137 4.0 7.7 1.0 CA A:GLN136 4.0 7.1 1.0 O A:HOH637 4.1 29.5 1.0 O A:VAL134 4.1 9.8 1.0 C A:GLN135 4.2 8.0 1.0 N A:GLU204 4.2 5.5 1.0 O A:HOH706 4.2 16.6 0.5 C3 A:HGB304 4.3 9.4 0.5 CA A:GLU204 4.3 5.3 1.0 C4 A:HGB304 4.4 10.0 0.5 C A:VAL134 4.5 8.1 1.0 O A:GLN135 4.6 9.4 1.0 CA A:GLN135 4.7 8.8 1.0 N A:GLN135 4.9 8.3 1.0 CD A:PRO137 4.9 8.8 1.0 C A:LEU203 4.9 5.0 1.0 C2 A:HGB304 4.9 10.1 0.5 C A:CYS205 4.9 4.2 0.3 C A:PRO137 4.9 7.8 1.0 O A:HOH572 5.0 32.9 1.0 CB A:LEU203 5.0 6.5 1.0 CB A:GLU204 5.0 5.9 1.0 C A:CYS205 5.0 4.3 0.5

Mercury binding site 2 out of 2 in the Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex.


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure at 2.1 A Reolution of A Helical Aromatic Foldamer-Protein Complex. within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg309 b:5.9 occ:0.30 HG A:HGB304 1.3 5.9 0.5 SG A:CYS205 1.3 5.8 0.5 SG A:CYS205 2.3 5.9 0.3 O A:HOH531 2.5 15.2 1.0 CB A:CYS205 2.7 5.4 0.5 O A:VAL134 3.1 9.8 1.0 C7 A:HGB304 3.2 6.7 0.5 CB A:CYS205 3.2 6.1 0.5 O A:GLN136 3.3 7.2 1.0 CA A:CYS205 3.5 5.3 0.5 CA A:CYS205 3.5 5.5 0.5 C A:VAL134 3.6 8.1 1.0 N A:CYS205 3.6 5.5 0.5 N A:GLN136 3.7 7.7 1.0 O A:HOH445 3.7 13.4 1.0 N A:CYS205 3.7 4.7 0.5 C A:GLU204 3.8 5.5 1.0 O A:GLU204 3.8 7.5 1.0 C A:GLN136 3.9 6.9 1.0 CB A:LEU203 4.1 6.5 1.0 C A:GLN135 4.1 8.0 1.0 N A:GLU204 4.1 5.5 1.0 C6 A:HGB304 4.1 10.1 0.5 N A:GLN135 4.2 8.3 1.0 CA A:VAL134 4.2 7.7 1.0 C5 A:HGB304 4.2 9.4 0.5 CA A:GLN135 4.2 8.8 1.0 CA A:GLN136 4.4 7.1 1.0 O A:HOH637 4.4 29.5 1.0 C A:LEU203 4.5 5.0 1.0 CA A:GLU204 4.6 5.3 1.0 O A:ALA133 4.7 7.2 1.0 N A:PRO137 4.7 7.2 1.0 CA A:LEU203 4.8 5.5 1.0 O A:GLN135 4.9 9.4 1.0 C A:CYS205 4.9 4.2 0.3 CB A:VAL134 5.0 8.3 1.0 C A:CYS205 5.0 4.3 0.5 CA A:PRO137 5.0 7.7 1.0 CG A:LEU203 5.0 8.6 1.0

J.Buratto, C.Colombo, M.Stupfel, S.J.Dawson, C.Dolain, B.Langlois D'estaintot, L.Fischer, T.Granier, M.Laguerre, B.Gallois, I.Huc. Structure of A Complex Formed By A Protein and A Helical Aromatic Oligoamide Foldamer at 2.1 A Resolution. Angew.Chem.Int.Ed.Engl. V. 53 883 2014.
ISSN: ISSN 1433-7851
PubMed: 24288253
DOI: 10.1002/ANIE.201309160