Mercury in PDB 4o93: Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer

All present enzymatic activity of Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer:
1.6.1.2;

The structure of Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer, PDB code: 4o93 was solved by J.H.Leung, M.Yamaguchi, A.Moeller, L.A.Schurig-Briccio, R.B.Gennis, C.S.Potter, B.Carragher, C.D.Stout, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	98.67 / 2.77
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	125.408, 86.920, 98.978, 90.00, 94.55, 90.00
R / Rfree (%)	20.4 / 26.9

The binding sites of Mercury atom in the Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer (pdb code 4o93). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer, PDB code: 4o93:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer


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 Thermus Thermophilis Transhydrogeanse Domain II Dimer within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg500 b:78.3 occ:0.60 SG A:CYS16 2.2 72.9 1.0 O A:CYS16 3.0 61.6 1.0 C A:CYS16 3.1 67.9 1.0 CB A:CYS16 3.2 64.2 1.0 N A:PHE17 3.5 65.0 1.0 CA A:CYS16 3.6 67.0 1.0 CA A:PHE17 3.9 64.7 1.0 CB A:TYR20 4.4 73.6 1.0 CG A:PHE17 4.7 71.8 1.0 CD1 A:PHE17 4.7 74.3 1.0 CD2 A:TYR20 4.7 82.6 1.0 CB B:ALA239 4.8 71.0 1.0 CG A:TYR20 4.9 83.3 1.0 CB A:PHE17 4.9 67.6 1.0 N A:CYS16 5.0 70.3 1.0 C A:PHE17 5.0 68.8 1.0

Mercury binding site 2 out of 2 in the Crystal Structure of Thermus Thermophilis Transhydrogeanse Domain II Dimer


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 Thermus Thermophilis Transhydrogeanse Domain II Dimer within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg500 b:82.3 occ:0.60 SG C:CYS16 2.1 78.5 1.0 O C:CYS16 3.0 84.1 1.0 C C:CYS16 3.1 74.7 1.0 CB C:CYS16 3.2 74.6 1.0 N C:PHE17 3.5 81.9 1.0 CA C:CYS16 3.7 72.8 1.0 CA C:PHE17 4.0 80.7 1.0 CB C:TYR20 4.6 82.9 1.0 CB D:ALA239 4.6 77.2 1.0 CG C:PHE17 4.7 78.5 1.0 CD2 C:PHE17 4.8 77.8 1.0 CD1 C:PHE17 4.9 87.2 1.0 CB C:PHE17 4.9 76.7 1.0 CD2 C:TYR20 4.9 98.7 1.0 O C:VAL13 5.0 78.0 1.0

J.H.Leung, L.A.Schurig-Briccio, M.Yamaguchi, A.Moeller, J.A.Speir, R.B.Gennis, C.D.Stout. Structural Biology. Division of Labor in Transhydrogenase By Alternating Proton Translocation and Hydride Transfer. Science V. 347 178 2015.
ISSN: ISSN 0036-8075
PubMed: 25574024
DOI: 10.1126/SCIENCE.1260451