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Mercury in PDB 3pyk: Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor

Enzymatic activity of Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor

All present enzymatic activity of Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor, PDB code: 3pyk was solved by T.Heinisch, T.Schirmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.60 / 1.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.099, 41.493, 72.382, 90.00, 104.33, 90.00
R / Rfree (%) 12.8 / 16.5

Other elements in 3pyk:

The structure of Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Ruthenium (Ru) 1 atom
Chlorine (Cl) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor (pdb code 3pyk). 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 Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor, PDB code: 3pyk:

Mercury binding site 1 out of 1 in 3pyk

Go back to Mercury Binding Sites List in 3pyk
Mercury binding site 1 out of 1 in the Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II As Host For Pianostool Complexes Bearing A Sulfonamide Anchor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg264

b:13.1
occ:0.80
 HG A:MMC264 0.0 13.1 0.8
C A:MMC264 2.0 15.3 0.8
SG A:CYS206 2.3 6.0 0.5
CB A:CYS206 3.0 11.0 0.5
O A:GLN137 3.0 9.0 1.0
O A:HOH524 3.1 20.4 1.0
CB A:CYS206 3.2 5.2 0.5
O A:GLU205 3.3 8.2 1.0
O A:VAL135 3.4 12.1 1.0
N A:GLN137 3.5 8.7 1.0
C A:GLU205 3.5 6.3 1.0
C A:GLN137 3.5 9.0 1.0
CA A:CYS206 3.5 4.8 0.5
CA A:CYS206 3.5 9.1 0.5
N A:CYS206 3.7 7.4 0.5
N A:CYS206 3.7 6.0 0.5
C A:VAL135 3.8 8.5 1.0
O A:HOH509 3.9 19.4 1.0
C A:GLN136 3.9 9.2 1.0
N A:GLU205 4.1 7.4 1.0
CA A:GLN137 4.1 8.5 1.0
SG A:CYS206 4.1 26.7 0.5
N A:PRO138 4.2 9.0 1.0
CA A:GLN136 4.3 8.8 1.0
N A:GLN136 4.3 9.4 1.0
CA A:GLU205 4.4 6.6 1.0
CA A:PRO138 4.4 9.3 1.0
CA A:VAL135 4.5 9.0 1.0
O A:GLN136 4.5 11.7 1.0
O A:HOH436 4.6 13.6 1.0
CB A:LEU204 4.6 8.6 1.0
C A:LEU204 4.7 6.9 1.0
O A:ALA134 4.8 8.0 1.0
O A:HOH291 4.8 0.8 1.0
C A:CYS206 5.0 6.0 0.5
C A:CYS206 5.0 8.0 0.5

Reference:

F.W.Monnard, T.Heinisch, E.S.Nogueira, T.Schirmer, T.R.Ward. Human Carbonic Anhydrase II As A Host For Piano-Stool Complexes Bearing A Sulfonamide Anchor. Chem.Commun.(Camb.) V. 47 8238 2011.
ISSN: ISSN 1359-7345
PubMed: 21706094
DOI: 10.1039/C1CC10345H
Page generated: Fri Aug 8 10:15:12 2025

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