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Mercury in PDB 1g1d: Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide

Enzymatic activity of Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide

All present enzymatic activity of Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide, PDB code: 1g1d was solved by C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.04
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.790, 41.860, 72.730, 90.00, 104.70, 90.00
R / Rfree (%) 19.8 / 27.7

Other elements in 1g1d:

The structure of Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide also contains other interesting chemical elements:

Fluorine (F) 1 atom
Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide (pdb code 1g1d). 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 II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide, PDB code: 1g1d:

Mercury binding site 1 out of 1 in 1g1d

Go back to Mercury Binding Sites List in 1g1d
Mercury binding site 1 out of 1 in the Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg263

b:1.3
occ:1.00
SG A:CYS206 1.6 27.6 1.0
CB A:CYS206 2.8 11.2 1.0
O A:GLN137 3.1 13.4 1.0
CA A:CYS206 3.1 11.3 1.0
O A:VAL135 3.3 23.1 1.0
O A:GLU205 3.3 4.8 1.0
N A:CYS206 3.4 9.3 1.0
C A:GLU205 3.4 8.2 1.0
C A:GLN137 3.5 14.2 1.0
N A:GLN137 3.6 15.5 1.0
O A:HOH299 3.7 16.9 1.0
C A:VAL135 3.9 20.4 1.0
CA A:GLN137 4.1 18.5 1.0
C A:GLN136 4.2 13.5 1.0
N A:GLU205 4.2 5.3 1.0
N A:PRO138 4.2 14.8 1.0
O A:HOH309 4.3 36.2 1.0
CA A:GLU205 4.5 6.3 1.0
CA A:GLN136 4.5 17.2 1.0
CB A:LEU204 4.5 9.9 1.0
CA A:PRO138 4.5 12.6 1.0
N A:GLN136 4.5 15.7 1.0
O A:HOH291 4.6 24.8 1.0
C A:LEU204 4.6 7.0 1.0
C A:CYS206 4.6 10.2 1.0
CA A:VAL135 4.8 19.5 1.0
O A:GLN136 4.9 11.0 1.0
O A:ALA134 5.0 19.5 1.0

Reference:

C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson. Contribution of Fluorine to Protein-Ligand Affinity in the Binding of Fluoroaromatic Inhibitors to Carbonic Anhydrase II J.Am.Chem.Soc. V. 122 12125 2000.
ISSN: ISSN 0002-7863
DOI: 10.1021/JA002627N
Page generated: Sun Dec 13 19:02:45 2020

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