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Mercury in PDB 2f14: Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor

Enzymatic activity of Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor

All present enzymatic activity of Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor:
4.2.1.1;

Protein crystallography data

The structure of Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor, PDB code: 2f14 was solved by V.Alterio, C.Pedone, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.71
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.260, 41.600, 72.220, 90.00, 104.57, 90.00
R / Rfree (%) 17.2 / 20.2

Other elements in 2f14:

The structure of Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor (pdb code 2f14). 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 Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor, PDB code: 2f14:

Mercury binding site 1 out of 1 in 2f14

Go back to Mercury Binding Sites List in 2f14
Mercury binding site 1 out of 1 in the Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Tne Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Fluorescent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1206

b:18.1
occ:1.00
 HG A:HGB1206 0.0 18.1 1.0
SG A:CYS206 2.0 13.4 1.0
C7 A:HGB1206 2.0 17.4 1.0
O A:HOH1395 2.9 22.9 1.0
O A:GLN137 3.0 11.6 1.0
CB A:CYS206 3.0 14.3 1.0
C5 A:HGB1206 3.0 20.3 1.0
C6 A:HGB1206 3.0 19.5 1.0
O A:GLU205 3.2 9.0 1.0
C A:GLN137 3.4 12.3 1.0
CA A:CYS206 3.4 9.8 1.0
C A:GLU205 3.4 9.5 1.0
N A:CYS206 3.5 10.8 1.0
O A:HOH1314 3.7 14.1 1.0
N A:GLN137 3.8 12.8 1.0
N A:PRO138 3.9 11.9 1.0
O A:VAL135 4.0 13.9 1.0
C A:GLN136 4.1 15.2 1.0
CA A:GLN137 4.1 11.6 1.0
CA A:PRO138 4.1 12.4 1.0
N A:GLU205 4.3 8.6 1.0
C4 A:HGB1206 4.3 19.4 1.0
C3 A:HGB1206 4.3 19.9 1.0
C A:VAL135 4.4 14.2 1.0
CA A:GLU205 4.4 7.7 1.0
CA A:GLN136 4.5 16.1 1.0
N A:GLN136 4.6 15.2 1.0
O A:GLN136 4.6 15.1 1.0
C2 A:HGB1206 4.9 19.9 1.0
C A:CYS206 4.9 10.8 1.0
C A:LEU204 4.9 9.3 1.0
CB A:LEU204 5.0 10.9 1.0
CD A:PRO138 5.0 13.8 1.0

Reference:

V.Alterio, R.M.Vitale, S.M.Monti, C.Pedone, A.Scozzafava, A.Cecchi, G.De Simone, C.T.Supuran. Carbonic Anhydrase Inhibitors: X-Ray and Molecular Modeling Study For the Interaction of A Fluorescent Antitumor Sulfonamide with Isozyme II and IX. J.Am.Chem.Soc. V. 128 8329 2006.
ISSN: ISSN 0002-7863
PubMed: 16787097
DOI: 10.1021/JA061574S
Page generated: Fri Aug 8 09:48:27 2025

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