Atomistry » Mercury » PDB 1g52-1irk » 1if5
Atomistry »
  Mercury »
    PDB 1g52-1irk »
      1if5 »

Mercury in PDB 1if5: Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

Enzymatic activity of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

All present enzymatic activity of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide, PDB code: 1if5 was solved by C.-Y.Kim, D.W.Christianson, 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 (°) 43.200, 42.700, 73.300, 90.00, 104.58, 90.00
R / Rfree (%) 22.1 / 28.7

Other elements in 1if5:

The structure of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide (pdb code 1if5). 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 Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide, PDB code: 1if5:

Mercury binding site 1 out of 1 in 1if5

Go back to Mercury Binding Sites List in 1if5
Mercury binding site 1 out of 1 in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:20.2
occ:1.00
 SG A:CYS206 1.6 23.5 1.0
CB A:CYS206 2.8 14.6 1.0
O A:GLN137 3.2 14.4 1.0
O A:VAL135 3.3 19.9 1.0
CA A:CYS206 3.4 13.0 1.0
O A:GLU205 3.5 9.8 1.0
N A:CYS206 3.6 9.0 1.0
C A:GLU205 3.6 9.3 1.0
C A:GLN137 3.6 16.9 1.0
N A:GLN137 3.7 19.0 1.0
C A:VAL135 3.9 18.9 1.0
C A:GLN136 4.0 18.4 1.0
O A:HOH310 4.0 41.0 1.0
O A:HOH322 4.1 20.4 1.0
CA A:GLN137 4.2 18.8 1.0
CA A:GLN136 4.3 18.4 1.0
N A:PRO138 4.3 16.8 1.0
N A:GLU205 4.3 8.2 1.0
N A:GLN136 4.4 16.7 1.0
O A:GLN136 4.5 19.1 1.0
O A:HOH280 4.5 20.2 1.0
CA A:GLU205 4.5 7.7 1.0
CA A:PRO138 4.6 15.4 1.0
CB A:LEU204 4.6 10.0 1.0
CA A:VAL135 4.8 17.1 1.0
C A:LEU204 4.8 9.2 1.0
C A:CYS206 4.9 10.9 1.0
O A:ALA134 5.0 17.4 1.0

Reference:

C.-Y.Kim, D.W.Christianson. Binding of Fluorine Substituted Benzenesulfonamides to Carbonic Anhydrase II To Be Published.
Page generated: Sun Aug 11 00:02:39 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy