Atomistry » Mercury » PDB 4ihd-4q7w » 4js6
Atomistry »
  Mercury »
    PDB 4ihd-4q7w »
      4js6 »

Mercury in PDB 4js6: Crystal Structure of Inhibitor-Free Hcaii H94D

Enzymatic activity of Crystal Structure of Inhibitor-Free Hcaii H94D

All present enzymatic activity of Crystal Structure of Inhibitor-Free Hcaii H94D:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Inhibitor-Free Hcaii H94D, PDB code: 4js6 was solved by D.P.Martin, Z.S.Hann, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.48 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.804, 41.217, 71.895, 90.00, 104.46, 90.00
R / Rfree (%) 18.4 / 22.2

Other elements in 4js6:

The structure of Crystal Structure of Inhibitor-Free Hcaii H94D also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of Inhibitor-Free Hcaii H94D (pdb code 4js6). 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 Inhibitor-Free Hcaii H94D, PDB code: 4js6:

Mercury binding site 1 out of 1 in 4js6

Go back to Mercury Binding Sites List in 4js6
Mercury binding site 1 out of 1 in the Crystal Structure of Inhibitor-Free Hcaii H94D


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 Inhibitor-Free Hcaii H94D within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg302

b:16.3
occ:0.50
HG A:MBO302 0.0 16.3 0.5
CE5 A:MBO302 2.3 7.6 0.5
SG A:CYS206 2.4 10.5 0.5
O A:GLN137 3.0 8.1 1.0
O A:VAL135 3.0 17.3 1.0
CB A:CYS206 3.1 6.3 0.5
CE2 A:MBO302 3.1 15.7 0.5
CB A:CYS206 3.3 6.6 0.5
CE1 A:MBO302 3.3 13.6 0.5
O A:GLU205 3.3 8.7 1.0
C A:GLN137 3.4 9.2 1.0
CA A:CYS206 3.5 5.7 0.5
CA A:CYS206 3.5 6.1 0.5
N A:GLN137 3.5 10.3 1.0
C A:GLU205 3.5 6.2 1.0
N A:CYS206 3.7 6.4 1.0
C A:VAL135 3.9 13.1 1.0
O A:HOH506 3.9 22.1 1.0
C A:GLN136 3.9 14.9 1.0
CA A:GLN137 4.0 9.8 1.0
N A:PRO138 4.1 9.5 1.0
N A:GLU205 4.2 8.4 1.0
CA A:PRO138 4.2 9.4 1.0
SG A:CYS206 4.2 7.2 0.5
CA A:GLN136 4.4 14.4 1.0
CA A:GLU205 4.4 7.5 1.0
CE4 A:MBO302 4.5 13.9 0.5
O A:GLN136 4.5 15.3 1.0
N A:GLN136 4.5 12.8 1.0
CE3 A:MBO302 4.6 18.3 0.5
CB A:LEU204 4.7 9.3 1.0
CA A:VAL135 4.8 11.8 1.0
C A:LEU204 4.8 8.1 1.0
C A:CYS206 4.9 6.3 1.0
O A:ALA134 4.9 8.3 1.0

Reference:

D.P.Martin, Z.S.Hann, S.M.Cohen. Metalloprotein-Inhibitor Binding: Human Carbonic Anhydrase II As A Model For Probing Metal-Ligand Interactions in A Metalloprotein Active Site. Inorg.Chem. V. 52 12207 2013.
ISSN: ISSN 0020-1669
PubMed: 23706138
DOI: 10.1021/IC400295F
Page generated: Sun Dec 13 19:11:16 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