Mercury in PDB 6cvl: Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein

The structure of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein, PDB code: 6cvl was solved by P.T.Nguyen, J.T.Kaiser, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.85 / 2.95
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	107.960, 107.960, 354.520, 90.00, 90.00, 120.00
R / Rfree (%)	20.8 / 22.6

The structure of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein also contains other interesting chemical elements:

Iodine

(I)

2 atoms

The binding sites of Mercury atom in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein (pdb code 6cvl). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein, PDB code: 6cvl:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg401 b:0.3 occ:1.00 HE1 C:HIS0 2.7 0.6 1.0 CE1 C:HIS0 3.2 0.2 1.0 ND1 C:HIS0 3.3 0.5 1.0 H1 C:HIS0 3.5 0.2 1.0 N C:HIS0 4.4 0.1 1.0 NE2 C:HIS0 4.4 0.9 1.0 H3 C:HIS0 4.6 0.2 1.0 CG C:HIS0 4.6 0.1 1.0 HB3 C:PRO29 4.7 97.5 1.0 H2 C:HIS0 4.8 0.2 1.0 HE2 C:HIS0 4.9 0.3 1.0

Mercury binding site 2 out of 3 in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg402 b:0.8 occ:1.00 HG C:CYS164 2.0 81.3 1.0 HB3 C:ALA167 2.8 75.0 1.0 SG C:CYS164 3.0 70.1 1.0 HD11 C:LEU183 3.1 0.0 1.0 HB3 C:CYS164 3.1 85.9 1.0 CB C:CYS164 3.5 73.0 1.0 HD13 C:LEU183 3.5 0.0 1.0 HB2 C:CYS164 3.5 85.9 1.0 CD1 C:LEU183 3.7 98.1 1.0 CB C:ALA167 3.8 60.1 1.0 HB2 C:LEU196 3.8 83.1 1.0 HD22 C:LEU196 3.8 86.7 1.0 HG23 C:THR168 3.8 78.9 1.0 HB2 C:ALA167 4.0 75.0 1.0 HD12 C:LEU183 4.0 0.0 1.0 HB3 C:LEU196 4.0 83.1 1.0 H C:ALA167 4.1 76.5 1.0 HB1 C:ALA167 4.1 75.0 1.0 HD21 C:LEU180 4.2 0.0 1.0 HD23 C:LEU180 4.3 0.0 1.0 CB C:LEU196 4.3 69.5 1.0 HD11 C:ILE207 4.6 0.8 1.0 CD2 C:LEU180 4.6 95.6 1.0 HG21 C:ILE194 4.6 84.4 1.0 CD2 C:LEU196 4.7 74.9 1.0 HD22 C:LEU180 4.7 0.0 1.0 CG2 C:THR168 4.7 67.8 1.0 HG21 C:THR168 4.7 78.9 1.0 HD21 C:LEU183 4.7 0.2 1.0 HD12 C:ILE87 4.7 70.4 1.0 CA C:ALA167 4.8 59.7 1.0 N C:ALA167 4.8 60.2 1.0 HD13 C:LEU196 4.9 85.4 1.0 HD23 C:LEU196 4.9 86.7 1.0 CA C:CYS164 5.0 73.8 1.0 HD22 C:LEU183 5.0 0.2 1.0 HG11 C:VAL203 5.0 88.0 1.0 HD21 C:LEU162 5.0 0.9 1.0 CG C:LEU183 5.0 95.4 1.0

Mercury binding site 3 out of 3 in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ D:Hg401 b:0.9 occ:1.00 I D:IOD403 2.5 0.6 1.0 HB3 D:ALA167 3.1 79.8 1.0 H D:ALA167 3.3 77.6 1.0 HD22 D:LEU196 3.4 80.0 1.0 HG1 D:THR168 3.4 78.5 1.0 HB2 D:LEU196 3.4 78.3 1.0 HB3 D:CYS164 3.4 75.2 1.0 HD13 D:LEU196 3.6 79.7 1.0 HG11 D:VAL203 3.6 86.8 1.0 HG D:CYS164 3.7 80.8 1.0 HB2 D:CYS164 3.7 75.2 1.0 CB D:CYS164 3.9 58.3 1.0 HD21 D:LEU180 3.9 93.0 1.0 N D:ALA167 4.0 66.1 1.0 CB D:ALA167 4.0 68.9 1.0 H D:THR168 4.1 77.2 1.0 I D:IOD402 4.2 0.8 1.0 CB D:LEU196 4.2 59.2 1.0 OG1 D:THR168 4.2 73.8 1.0 SG D:CYS164 4.2 65.1 1.0 CD2 D:LEU196 4.3 62.7 1.0 HB3 D:LEU196 4.3 78.3 1.0 CD1 D:LEU196 4.4 61.3 1.0 N D:THR168 4.4 70.7 1.0 CA D:ALA167 4.4 66.7 1.0 CG D:LEU196 4.5 61.6 1.0 HB2 D:ALA167 4.5 79.8 1.0 HD11 D:LEU196 4.5 79.7 1.0 CG1 D:VAL203 4.5 76.9 1.0 HD11 D:LEU183 4.5 98.5 1.0 HB1 D:ALA167 4.6 79.8 1.0 CD2 D:LEU180 4.6 73.8 1.0 C D:ALA167 4.6 66.3 1.0 HA D:GLN166 4.6 76.4 1.0 HD23 D:LEU180 4.6 93.0 1.0 HD22 D:LEU180 4.7 93.0 1.0 HB D:THR198 4.7 74.3 1.0 HD11 D:ILE207 4.7 0.1 1.0 HG13 D:VAL203 4.7 86.8 1.0 O D:ILE197 4.7 57.4 1.0 HD23 D:LEU196 4.8 80.0 1.0 CB D:THR168 4.8 71.9 1.0 HD21 D:LEU196 4.8 80.0 1.0 HG12 D:VAL203 4.8 86.8 1.0 HG21 D:VAL203 4.8 84.2 1.0 HD13 D:LEU183 4.9 98.5 1.0 H D:GLN166 5.0 75.1 1.0 C D:GLN166 5.0 62.3 1.0

P.T.Nguyen, J.Y.Lai, A.T.Lee, J.T.Kaiser, D.C.Rees. Noncanonical Role For the Binding Protein in Substrate Uptake By the Metni Methionine Atp Binding Cassette (Abc) Transporter. Proc. Natl. Acad. Sci. V. 115 10596 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30352853
DOI: 10.1073/PNAS.1811003115