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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: Wed Oct 28 18:38:57 2020

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