Mercury in PDB 1bh9: HTAFII18/HTAFII28 Heterodimer Crystal Structure with Bound Pcmbs

The structure of HTAFII18/HTAFII28 Heterodimer Crystal Structure with Bound Pcmbs, PDB code: 1bh9 was solved by C.Birck, O.Poch, C.Romier, M.Ruff, G.Mengus, A.-C.Lavigne, I.Davidson, D.Moras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.800, 48.400, 70.100, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 25.7

The binding sites of Mercury atom in the HTAFII18/HTAFII28 Heterodimer Crystal Structure with Bound Pcmbs (pdb code 1bh9). 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 HTAFII18/HTAFII28 Heterodimer Crystal Structure with Bound Pcmbs, PDB code: 1bh9:

Mercury binding site 1 out of 1 in the HTAFII18/HTAFII28 Heterodimer Crystal Structure with Bound Pcmbs


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of HTAFII18/HTAFII28 Heterodimer Crystal Structure with Bound Pcmbs within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg300 b:50.3 occ:1.00 HG B:PMB300 0.0 50.3 1.0 C4 B:PMB300 1.9 50.6 1.0 SG B:CYS173 2.7 42.1 1.0 C3 B:PMB300 2.7 50.3 1.0 C5 B:PMB300 2.9 50.3 1.0 CB B:CYS173 3.1 37.5 1.0 O B:GLU178 3.1 32.1 1.0 C B:CYS173 3.2 37.5 1.0 N B:GLU174 3.2 37.6 1.0 O B:CYS173 3.4 38.0 1.0 CA B:GLU174 3.7 40.8 1.0 CA B:MET179 3.7 35.1 1.0 CA B:CYS173 3.7 37.6 1.0 C B:GLU178 3.7 34.5 1.0 CD B:PRO180 3.7 33.5 1.0 N B:PRO180 3.8 34.2 1.0 C B:MET179 3.8 34.5 1.0 CG B:PRO180 3.9 32.8 1.0 O B:LEU170 3.9 37.4 1.0 N B:MET179 4.0 35.2 1.0 C2 B:PMB300 4.1 50.5 1.0 C6 B:PMB300 4.2 51.2 1.0 CB B:GLU174 4.3 43.4 1.0 O B:MET179 4.5 33.0 1.0 CA B:PRO180 4.6 34.8 1.0 C1 B:PMB300 4.7 52.1 1.0 N B:CYS173 4.7 38.1 1.0 CA B:GLU178 4.9 36.0 1.0 C B:LEU170 4.9 37.2 1.0 CB B:PRO180 5.0 34.2 1.0

C.Birck, O.Poch, C.Romier, M.Ruff, G.Mengus, A.C.Lavigne, I.Davidson, D.Moras. Human Taf(II)28 and Taf(II)18 Interact Through A Histone Fold Encoded By Atypical Evolutionary Conserved Motifs Also Found in the SPT3 Family. Cell(Cambridge,Mass.) V. 94 239 1998.
ISSN: ISSN 0092-8674
PubMed: 9695952
DOI: 10.1016/S0092-8674(00)81423-3