Atomistry » Mercury » PDB 12ca-1czm » 1cni
Atomistry »
  Mercury »
    PDB 12ca-1czm »
      1cni »

Mercury in PDB 1cni: X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site

Enzymatic activity of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site

All present enzymatic activity of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site:
4.2.1.1;

Protein crystallography data

The structure of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site, PDB code: 1cni was solved by C.A.Lesburg, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) 16.1 / n/a

Other elements in 1cni:

The structure of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site (pdb code 1cni). 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 X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site, PDB code: 1cni:

Mercury binding site 1 out of 1 in 1cni

Go back to Mercury Binding Sites List in 1cni
Mercury binding site 1 out of 1 in the X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg262

b:19.6
occ:1.00
SG A:CYS206 2.3 19.2 1.0
O A:GLN137 3.0 13.0 1.0
CB A:CYS206 3.1 12.7 1.0
O A:GLU205 3.4 7.7 1.0
C A:GLN137 3.4 13.6 1.0
O A:VAL135 3.5 14.9 1.0
CA A:CYS206 3.6 8.9 1.0
C A:GLU205 3.7 8.6 1.0
N A:GLN137 3.7 15.2 1.0
N A:CYS206 3.8 8.7 1.0
C A:GLN136 3.9 16.4 1.0
C A:VAL135 4.0 14.8 1.0
N A:PRO138 4.1 12.9 1.0
CA A:GLN137 4.1 13.9 1.0
O A:HOH318 4.2 22.8 1.0
CA A:GLN136 4.3 16.4 1.0
CA A:PRO138 4.3 11.4 1.0
N A:GLN136 4.4 15.0 1.0
O A:GLN136 4.4 16.4 1.0
O A:HOH325 4.4 17.0 1.0
N A:GLU205 4.5 8.6 1.0
CA A:GLU205 4.6 7.7 1.0
O A:HOH391 4.6 43.1 1.0
CA A:VAL135 4.8 14.4 1.0
CB A:LEU204 4.9 12.3 1.0
O A:ALA134 5.0 13.6 1.0

Reference:

C.A.Lesburg, D.W.Christianson. X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in A Protein-Zinc Binding Site J.Am.Chem.Soc. V. 117 6838 1995.
ISSN: ISSN 0002-7863
Page generated: Sun Dec 13 19:02:13 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy