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

Mercury in PDB 1can: Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions

Enzymatic activity of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions

All present enzymatic activity of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions:
4.2.1.1;

Protein crystallography data

The structure of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions, PDB code: 1can was solved by S.Mangani, K.Hakansson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
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 (%) n/a / n/a

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions (pdb code 1can). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions, PDB code: 1can:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 1can

Go back to Mercury Binding Sites List in 1can
Mercury binding site 1 out of 2 in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg262

b:7.4
occ:1.00
O A:HOH263 1.9 6.5 1.0
ND1 A:HIS119 2.0 3.5 1.0
NE2 A:HIS96 2.1 4.6 1.0
NE2 A:HIS94 2.1 9.8 1.0
O2 A:NO3511 2.8 18.6 0.7
CE1 A:HIS119 2.9 4.5 1.0
CE1 A:HIS96 3.0 5.4 1.0
CD2 A:HIS96 3.0 3.8 1.0
CD2 A:HIS94 3.1 6.9 1.0
CE1 A:HIS94 3.1 4.7 1.0
CG A:HIS119 3.1 6.4 1.0
CB A:HIS119 3.6 3.1 1.0
N A:NO3511 3.7 18.2 0.7
OG1 A:THR199 3.8 6.0 1.0
O A:HOH338 3.9 17.5 0.3
OE1 A:GLU106 4.0 6.6 1.0
O3 A:NO3511 4.0 28.1 0.7
NE2 A:HIS119 4.1 4.7 1.0
O A:HOH318 4.1 31.5 1.0
ND1 A:HIS96 4.2 3.6 1.0
CG A:HIS96 4.2 3.9 1.0
CD2 A:HIS119 4.2 6.4 1.0
CG A:HIS94 4.3 9.6 1.0
ND1 A:HIS94 4.3 9.6 1.0
O A:HOH292 4.3 29.8 1.0
O1 A:NO3511 4.6 28.6 0.7
CD A:GLU106 4.9 8.6 1.0

Mercury binding site 2 out of 2 in 1can

Go back to Mercury Binding Sites List in 1can
Mercury binding site 2 out of 2 in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg510

b:12.3
occ:0.20
O A:HOH362 2.1 33.0 1.0
O A:HOH448 2.2 28.6 1.0
O A:VAL135 2.9 14.1 1.0
CB A:CYS206 2.9 9.8 1.0
O A:GLN137 3.1 13.2 1.0
N A:GLN137 3.3 7.4 1.0
C A:GLN137 3.4 12.2 1.0
C A:GLN136 3.4 21.6 1.0
CA A:CYS206 3.4 10.4 1.0
O A:GLU205 3.5 10.3 1.0
C A:GLU205 3.6 6.6 1.0
N A:CYS206 3.8 4.2 1.0
O A:HOH331 3.8 11.9 1.0
O A:GLN136 3.8 19.5 1.0
C A:VAL135 3.8 21.0 1.0
CA A:GLN137 3.9 6.5 1.0
CA A:GLN136 3.9 8.9 1.0
N A:PRO138 4.0 9.6 1.0
O A:HOH365 4.1 36.6 1.0
N A:GLN136 4.3 7.1 1.0
SG A:CYS206 4.3 14.3 1.0
N A:GLU205 4.3 8.8 1.0
O A:HOH507 4.4 37.3 1.0
CA A:PRO138 4.4 7.8 1.0
CA A:GLU205 4.6 4.1 1.0
CB A:LEU204 4.6 8.6 1.0
C A:LEU204 4.8 3.1 1.0
CD A:PRO138 4.9 20.2 1.0
C A:CYS206 4.9 8.2 1.0
CA A:VAL135 4.9 15.4 1.0

Reference:

S.Mangani, K.Hakansson. Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions. Eur.J.Biochem. V. 210 867 1992.
ISSN: ISSN 0014-2956
PubMed: 1336460
DOI: 10.1111/J.1432-1033.1992.TB17490.X
Page generated: Sun Dec 13 19:02:10 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