Mercury in PDB 2fmg: Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine

Enzymatic activity of Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine

All present enzymatic activity of Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine, PDB code: 2fmg 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)*	15.00 / 1.60
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	41.990, 41.410, 72.200, 90.00, 104.40, 90.00
*R / R_free (%)*	22 / 24

Other elements in 2fmg:

The structure of Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine 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 Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine (pdb code 2fmg). 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 Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine, PDB code: 2fmg:

Mercury binding site 1 out of 1 in 2fmg

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Mercury Binding Sites List in 2fmg

Mercury binding site 1 out of 1 in the Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine

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 Isoforms I, II, IV, Va, VII and Xiv with L- and D- Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Sterospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design, Structure with L-Phenylalanine within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:12.7 occ:1.00	SG	A:CYS206	2.4	8.5	1.0
	O	A:HOH455	2.5	18.7	1.0
	O	A:HOH344	2.9	21.8	1.0
	O	A:GLN137	3.0	7.0	1.0
	O	A:GLU205	3.0	6.4	1.0
	CB	A:CYS206	3.1	9.0	1.0
	C	A:GLN137	3.4	7.0	1.0
	C	A:GLU205	3.4	5.6	1.0
	CA	A:CYS206	3.4	5.3	1.0
	O	A:HOH382	3.5	26.1	1.0
	N	A:CYS206	3.6	6.8	1.0
	N	A:GLN137	3.7	8.6	1.0
	N	A:PRO138	3.9	7.1	1.0
	O	A:HOH337	3.9	19.3	1.0
	O	A:VAL135	4.0	12.3	1.0
	CA	A:GLN137	4.1	7.0	1.0
	CA	A:PRO138	4.1	7.5	1.0
	C	A:GLN136	4.2	10.7	1.0
	C	A:VAL135	4.3	10.2	1.0
	N	A:GLU205	4.3	6.9	1.0
	CA	A:GLU205	4.4	6.5	1.0
	CA	A:GLN136	4.6	12.3	1.0
	N	A:GLN136	4.6	10.6	1.0
	O	A:GLN136	4.8	11.6	1.0
	O	A:HOH348	4.8	18.2	1.0
	C	A:CYS206	4.9	5.0	1.0
	CD	A:PRO138	4.9	9.5	1.0
	C	A:PRO138	5.0	5.9	1.0
	CB	A:GLU205	5.0	8.1	1.0

Reference:

C.Temperini, A.Scozzafava, D.Vullo, C.T.Supuran. Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, Va, VII, and Xiv with L- and D-Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Stereospecific Recognition Within the Active Site of An Enzyme and Its Consequences For the Drug Design. J.Med.Chem. V. 49 3019 2006.
ISSN: ISSN 0022-2623
PubMed: 16686544
DOI: 10.1021/JM0603320

Page generated: Sun Aug 11 02:33:12 2024

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