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Mercury in PDB 3k7k: Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions

Enzymatic activity of Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions

All present enzymatic activity of Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions, PDB code: 3k7k was solved by C.Temperini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.35 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.070, 41.410, 72.230, 90.00, 104.45, 90.00
R / Rfree (%) 19.4 / 24.8

Other elements in 3k7k:

The structure of Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions (pdb code 3k7k). 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 the Complex Between Carbonic Anhydrase II and Anions, PDB code: 3k7k:

Mercury binding site 1 out of 1 in 3k7k

Go back to Mercury Binding Sites List in 3k7k
Mercury binding site 1 out of 1 in the Crystal Structure of the Complex Between Carbonic Anhydrase II and Anions


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 Complex Between Carbonic Anhydrase II and Anions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:23.4
occ:1.00
SG A:CYS206 2.2 7.6 0.5
O A:HOH462 2.7 17.9 1.0
O A:GLN137 2.9 11.2 1.0
CB A:CYS206 3.1 8.3 0.5
O A:GLU205 3.2 8.1 1.0
CB A:CYS206 3.3 7.8 0.5
C A:GLN137 3.3 11.6 1.0
C A:GLU205 3.4 8.7 1.0
CA A:CYS206 3.4 8.3 0.5
CA A:CYS206 3.4 7.8 0.5
O A:HOH325 3.5 27.4 1.0
N A:CYS206 3.6 8.1 0.5
N A:CYS206 3.7 8.3 0.5
N A:GLN137 3.7 13.1 1.0
N A:PRO138 3.9 11.1 1.0
O A:VAL135 3.9 13.8 1.0
O A:HOH292 4.0 18.5 1.0
C A:GLN136 4.0 13.6 1.0
CA A:GLN137 4.1 12.4 1.0
CA A:PRO138 4.1 10.4 1.0
N A:GLU205 4.2 9.2 1.0
C A:VAL135 4.3 12.7 1.0
CA A:GLU205 4.4 9.0 1.0
SG A:CYS206 4.5 9.9 0.5
O A:GLN136 4.5 12.8 1.0
CA A:GLN136 4.5 14.1 1.0
O A:HOH466 4.6 26.0 1.0
N A:GLN136 4.6 13.2 1.0
C A:LEU204 4.8 9.5 1.0
C A:CYS206 4.9 7.8 0.5
C A:CYS206 4.9 7.6 0.5
CD A:PRO138 5.0 11.2 1.0
CB A:LEU204 5.0 9.9 1.0
CB A:GLU205 5.0 9.4 1.0
C A:PRO138 5.0 9.9 1.0
CA A:VAL135 5.0 12.1 1.0

Reference:

C.Temperini, A.Scozzafava, C.T.Supuran. Carbonic Anhydrase Inhibitors. X-Ray Crystal Studies of the Carbonic Anhydrase II-Trithiocarbonate Adduct-An Inhibitor Mimicking the Sulfonamide and Urea Binding to the Enzyme Bioorg.Med.Chem.Lett. V. 20 474 2010.
ISSN: ISSN 0960-894X
PubMed: 20005709
DOI: 10.1016/J.BMCL.2009.11.124
Page generated: Wed Oct 28 18:42:43 2020

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