Mercury in PDB 4p2a: Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain

The structure of Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain, PDB code: 4p2a was solved by T.Clairfeuille, M.Gallon, C.Mas, R.Ghai, R.Teasdale, P.Cullen, B.Collins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.91 / 2.70
Space group	P 3 1 2
Cell size a, b, c (Å), α, β, γ (°)	113.810, 113.810, 94.771, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / 25.9

The binding sites of Mercury atom in the Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain (pdb code 4p2a). 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 of Mouse VPS26A Bound to Rat SNX27 Pdz Domain, PDB code: 4p2a:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg401 b:0.5 occ:0.57 SG A:CYS173 2.3 0.6 1.0 CB A:CYS173 3.1 0.5 1.0 CB A:ARG201 4.1 0.1 1.0 CA A:CYS173 4.4 1.0 1.0 O A:ARG201 4.9 0.1 1.0 C A:ARG201 5.0 0.9 1.0

Mercury binding site 2 out of 2 in the Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure of Mouse VPS26A Bound to Rat SNX27 Pdz Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg402 b:0.2 occ:0.51 SG A:CYS12 2.4 0.8 1.0 CB A:CYS12 3.4 0.6 1.0 CA A:CYS12 4.7 0.7 1.0 C A:CYS12 4.8 0.1 1.0

M.Gallon, T.Clairfeuille, F.Steinberg, C.Mas, R.Ghai, R.B.Sessions, R.D.Teasdale, B.M.Collins, P.J.Cullen. A Unique Pdz Domain and Arrestin-Like Fold Interaction Reveals Mechanistic Details of Endocytic Recycling By SNX27-Retromer. Proc.Natl.Acad.Sci.Usa V. 111 E3604 2014.
ISSN: ESSN 1091-6490
PubMed: 25136126
DOI: 10.1073/PNAS.1410552111