Atomistry » Mercury » PDB 4q81-5c9l » 5bnl
Atomistry »
  Mercury »
    PDB 4q81-5c9l »
      5bnl »

Mercury in PDB 5bnl: Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins

Enzymatic activity of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins

All present enzymatic activity of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins:
4.2.1.1;

Protein crystallography data

The structure of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins, PDB code: 5bnl was solved by C.Temperini, A.Maresca, L.Pochet, B.Masereel, A.Scozzafava, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.230, 41.500, 72.420, 90.00, 104.50, 90.00
R / Rfree (%) 22.3 / 29.3

Other elements in 5bnl:

The structure of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins (pdb code 5bnl). 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 Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins, PDB code: 5bnl:

Mercury binding site 1 out of 1 in 5bnl

Go back to Mercury Binding Sites List in 5bnl
Mercury binding site 1 out of 1 in the Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg302

b:31.4
occ:1.00
O A:GLN137 3.0 11.3 1.0
O A:HOH467 3.1 24.6 1.0
CB A:CYS206 3.2 9.8 1.0
O A:GLU205 3.2 8.5 1.0
C A:GLN137 3.3 10.9 1.0
CA A:CYS206 3.5 9.7 1.0
C A:GLU205 3.5 8.0 1.0
O A:VAL135 3.6 14.6 1.0
N A:CYS206 3.7 9.0 1.0
N A:GLN137 3.7 11.5 1.0
N A:PRO138 3.8 10.9 1.0
C A:GLN136 3.9 12.3 1.0
O A:HOH503 4.0 11.8 1.0
CA A:GLN137 4.0 11.7 1.0
CA A:PRO138 4.0 10.6 1.0
C A:VAL135 4.1 12.3 1.0
N A:GLU205 4.2 6.5 1.0
O A:GLN136 4.4 11.8 1.0
CA A:GLU205 4.4 8.1 1.0
CA A:GLN136 4.4 12.2 1.0
N A:GLN136 4.6 12.0 1.0
SG A:CYS206 4.6 16.2 1.0
CB A:LEU204 4.8 5.7 1.0
C A:LEU204 4.8 6.3 1.0
CD A:PRO138 4.8 11.2 1.0
C A:CYS206 4.9 8.6 1.0
CA A:VAL135 5.0 11.6 1.0

Reference:

A.Maresca, C.Temperini, L.Pochet, B.Masereel, A.Scozzafava, C.T.Supuran. Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins. J.Med.Chem. V. 53 335 2010.
ISSN: ISSN 0022-2623
PubMed: 19911821
DOI: 10.1021/JM901287J
Page generated: Sun Dec 13 19:12:14 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy