Atomistry » Mercury » PDB 4ihd-4q7w » 4q7v
Atomistry »
  Mercury »
    PDB 4ihd-4q7w »
      4q7v »

Mercury in PDB 4q7v: Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II

Enzymatic activity of Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II

All present enzymatic activity of Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II, PDB code: 4q7v was solved by D.P.Martin, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.40 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.062, 41.168, 71.577, 90.00, 104.35, 90.00
R / Rfree (%) 16.7 / 21.2

Other elements in 4q7v:

The structure of Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II (pdb code 4q7v). 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 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II, PDB code: 4q7v:

Mercury binding site 1 out of 1 in 4q7v

Go back to Mercury Binding Sites List in 4q7v
Mercury binding site 1 out of 1 in the Crystal Structure of 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II


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 1-Hydroxy-5-Methylpyridine-2(1H)-Thione Bound to Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg303

b:17.9
occ:1.00
 HG A:MBO303 0.0 17.9 1.0
CE1 A:MBO303 2.2 18.8 1.0
SG A:CYS206 2.3 11.4 1.0
CE2 A:MBO303 3.0 21.7 1.0
O A:GLN137 3.0 6.2 1.0
O A:VAL135 3.0 13.4 1.0
CB A:CYS206 3.1 7.0 1.0
CE6 A:MBO303 3.1 17.4 1.0
CA A:CYS206 3.5 7.7 1.0
N A:GLN137 3.6 7.2 1.0
C A:GLN137 3.6 6.5 1.0
C A:VAL135 3.6 8.3 1.0
N A:CYS206 3.6 7.0 1.0
O A:GLU205 3.6 6.3 1.0
C A:GLU205 3.7 6.6 1.0
N A:GLU205 4.0 7.6 1.0
C A:GLN136 4.0 9.1 1.0
O A:HOH462 4.2 19.4 1.0
CB A:LEU204 4.2 6.6 1.0
CA A:GLN137 4.2 7.2 1.0
N A:GLN136 4.3 9.3 1.0
CE3 A:MBO303 4.3 25.9 1.0
CA A:VAL135 4.3 7.2 1.0
CA A:GLN136 4.3 9.8 1.0
N A:PRO138 4.4 7.6 1.0
CE5 A:MBO303 4.4 26.0 1.0
CA A:GLU205 4.5 7.3 1.0
C A:LEU204 4.5 5.4 1.0
CA A:PRO138 4.5 7.7 1.0
O A:ALA134 4.7 8.6 1.0
CE4 A:MBO303 4.8 27.8 1.0
O A:GLN136 4.8 10.3 1.0
CA A:LEU204 4.9 5.2 1.0
C A:CYS206 4.9 6.5 1.0
CB A:VAL135 5.0 7.9 1.0

Reference:

D.P.Martin, P.G.Blachly, J.A.Mccammon, S.M.Cohen. Exploring the Influence of the Protein Environment on Metal-Binding Pharmacophores. J.Med.Chem. V. 57 7126 2014.
ISSN: ISSN 0022-2623
PubMed: 25116076
DOI: 10.1021/JM500984B
Page generated: Fri Aug 8 10:36:58 2025

Last articles

Mn in 5NTD
Mn in 5O3N
Mn in 5O25
Mn in 5NSM
Mn in 5O1U
Mn in 5NTH
Mn in 5NTG
Mn in 5NSQ
Mn in 5NRZ
Mn in 5NMP
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy