Atomistry » Mercury » PDB 2esw-2o1f » 2foq
Atomistry »
  Mercury »
    PDB 2esw-2o1f »
      2foq »

Mercury in PDB 2foq: Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors

Enzymatic activity of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors

All present enzymatic activity of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors, PDB code: 2foq was solved by K.M.Jude, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.346, 41.359, 72.170, 90.00, 104.34, 90.00
R / Rfree (%) 16.4 / 21.3

Other elements in 2foq:

The structure of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors (pdb code 2foq). 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 Complexed with Two-Prong Inhibitors, PDB code: 2foq:

Mercury binding site 1 out of 1 in 2foq

Go back to Mercury Binding Sites List in 2foq
Mercury binding site 1 out of 1 in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors


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 Complexed with Two-Prong Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg206

b:18.8
occ:1.00
HG A:CMH206 0.0 18.8 1.0
CM A:CMH206 2.0 29.8 1.0
SG A:CMH206 2.3 17.1 1.0
O A:GLN137 3.0 11.2 1.0
O A:HOH548 3.0 25.3 1.0
CB A:CMH206 3.3 10.8 1.0
O A:GLU205 3.3 11.0 1.0
C A:GLN137 3.4 10.9 1.0
N A:GLN137 3.5 13.7 1.0
CA A:CMH206 3.6 9.4 1.0
C A:GLU205 3.6 9.8 1.0
O A:VAL135 3.6 16.2 1.0
O A:HOH444 3.8 17.8 1.0
N A:CMH206 3.8 8.9 1.0
C A:GLN136 3.8 15.3 1.0
CA A:GLN137 4.0 11.4 1.0
N A:PRO138 4.0 11.9 1.0
C A:VAL135 4.0 12.3 1.0
N A:GLU205 4.3 10.6 1.0
CA A:PRO138 4.3 11.0 1.0
CA A:GLN136 4.3 13.1 1.0
O A:GLN136 4.4 16.7 1.0
N A:GLN136 4.5 12.8 1.0
O A:HOH499 4.5 20.2 1.0
CA A:GLU205 4.5 8.9 1.0
CA A:VAL135 4.7 12.1 1.0
CB A:LEU204 4.7 10.4 1.0
C A:LEU204 4.9 9.6 1.0
O A:ALA134 4.9 11.6 1.0

Reference:

K.M.Jude, A.L.Banerjee, M.K.Haldar, S.Manokaran, B.Roy, S.Mallik, D.K.Srivastava, D.W.Christianson. Ultrahigh Resolution Crystal Structures of Human Carbonic Anhydrases I and II Complexed with Two-Prong Inhibitors Reveal the Molecular Basis of High Affinity. J.Am.Chem.Soc. V. 128 3011 2006.
ISSN: ISSN 0002-7863
PubMed: 16506782
DOI: 10.1021/JA057257N
Page generated: Wed Oct 28 18:41:30 2020

Last articles

Xe in 6AYK
Xe in 6QII
Xe in 6ASM
Xe in 5NSW
Xe in 6FY9
Xe in 5O1K
Xe in 5O27
Xe in 5M69
Xe in 5KPU
Xe in 5I63
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy