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Mercury in PDB 2ez7: Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme

Enzymatic activity of Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme

All present enzymatic activity of Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme, PDB code: 2ez7 was solved by C.Temperini, A.Scozzafava, D.Vullo, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.060, 41.430, 72.520, 90.00, 104.40, 90.00
R / Rfree (%) 24.9 / 30

Other elements in 2ez7:

The structure of Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme (pdb code 2ez7). 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 Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme, PDB code: 2ez7:

Mercury binding site 1 out of 1 in 2ez7

Go back to Mercury Binding Sites List in 2ez7
Mercury binding site 1 out of 1 in the Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton Transfer Processes Within the Active Site of An Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg483

b:12.8
occ:1.00
 O A:HOH485 2.7 1.4 1.0
O A:GLU205 2.9 4.0 1.0
O A:HOH529 2.9 1.0 1.0
O A:GLN137 3.0 8.8 1.0
CB A:CYS206 3.0 12.9 1.0
CA A:CYS206 3.4 10.0 1.0
C A:GLU205 3.4 4.2 1.0
C A:GLN137 3.4 10.9 1.0
N A:CYS206 3.7 3.9 1.0
N A:GLN137 3.8 12.7 1.0
SG A:CYS206 4.0 28.0 1.0
N A:PRO138 4.1 9.0 1.0
CA A:GLN137 4.1 12.4 1.0
O A:VAL135 4.2 11.2 1.0
C A:GLN136 4.3 13.4 1.0
CA A:PRO138 4.3 8.1 1.0
N A:GLU205 4.5 5.6 1.0
C A:VAL135 4.5 11.2 1.0
CA A:GLU205 4.5 5.2 1.0
CA A:GLN136 4.6 12.0 1.0
N A:GLN136 4.7 10.9 1.0
C A:CYS206 4.9 6.8 1.0
O A:GLN136 5.0 13.0 1.0
C A:LEU204 5.0 7.0 1.0

Reference:

C.Temperini, A.Scozzafava, D.Vullo, C.T.Supuran. Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, Va, VII, and Xiv with L- and D-Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton-Transfer Processes Within the Active Site of An Enzyme. Chemistry V. 12 7057 2006.
ISSN: ISSN 0947-6539
PubMed: 16807956
DOI: 10.1002/CHEM.200600159
Page generated: Wed Oct 28 18:41:27 2020

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