Mercury in PDB 5w31: Crystal Structure of Mutant Cj Ycei Protein (Cj-N48C) with Mercuribenzoic Acid Guest Structure

The structure of Crystal Structure of Mutant Cj Ycei Protein (Cj-N48C) with Mercuribenzoic Acid Guest Structure, PDB code: 5w31 was solved by T.R.Huber, C.D.Snow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.74 / 2.56
Space group	P 6 2 2
Cell size a, b, c (Å), α, β, γ (°)	178.793, 178.793, 50.814, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 24.1

The binding sites of Mercury atom in the Crystal Structure of Mutant Cj Ycei Protein (Cj-N48C) with Mercuribenzoic Acid Guest Structure (pdb code 5w31). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystal Structure of Mutant Cj Ycei Protein (Cj-N48C) with Mercuribenzoic Acid Guest Structure, PDB code: 5w31:

Mercury binding site 1 out of 1 in the Crystal Structure of Mutant Cj Ycei Protein (Cj-N48C) with Mercuribenzoic Acid Guest Structure


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 Mutant Cj Ycei Protein (Cj-N48C) with Mercuribenzoic Acid Guest Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg304 b:0.7 occ:0.85 HG A:MBO304 0.0 0.7 0.9 CE1 A:MBO304 2.3 0.8 0.9 SG A:CYS48 2.4 85.0 1.0 CE2 A:MBO304 3.2 0.8 0.9 CE6 A:MBO304 3.3 0.7 0.9 N A:CYS48 3.4 79.5 1.0 CB A:CYS48 3.4 73.4 1.0 O A:ASN78 3.6 73.3 1.0 ND2 A:ASN78 3.9 84.4 1.0 CA A:CYS48 3.9 78.6 1.0 C A:GLY47 3.9 78.9 1.0 CG A:ASN78 4.2 84.9 1.0 CA A:GLY47 4.3 75.9 1.0 CB A:ASN78 4.4 74.0 1.0 CE3 A:MBO304 4.5 0.0 0.9 C A:ASN78 4.5 78.2 1.0 CE5 A:MBO304 4.6 0.7 0.9 O A:GLY47 4.6 88.8 1.0 C A:CYS48 4.7 78.7 1.0 O A:CYS48 4.9 80.7 1.0 OD1 A:ASN78 4.9 95.3 1.0 N A:GLY47 5.0 81.6 1.0

T.R.Huber, E.C.Mcpherson, C.E.Keating, C.D.Snow. Installing Guest Molecules at Specific Sites Within Scaffold Protein Crystals. Bioconjug. Chem. V. 29 17 2018.
ISSN: ISSN 1520-4812
PubMed: 29232505
DOI: 10.1021/ACS.BIOCONJCHEM.7B00668