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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: Sat Aug 10 23:22:48 2024

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