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Zinc 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 / Rfree (%) 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:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc 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:

Zinc binding site 1 out of 1 in 2fmg

Go back to Zinc Binding Sites List in 2fmg
Zinc 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 Zinc with other atoms in the Zn 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:Zn262

b:6.3
occ:1.00
 ND1 A:HIS119 2.0 1.3 1.0
NE2 A:HIS94 2.1 4.1 1.0
NE2 A:HIS96 2.1 4.2 1.0
O A:HOH442 2.5 2.1 0.5
CE1 A:HIS119 2.9 2.9 1.0
CD2 A:HIS96 2.9 2.6 1.0
CD2 A:HIS94 3.0 5.2 1.0
CG A:HIS119 3.1 3.5 1.0
CE1 A:HIS94 3.1 3.6 1.0
CE1 A:HIS96 3.2 5.1 1.0
CB A:HIS119 3.5 3.9 1.0
OG1 A:THR199 3.5 2.0 1.0
O A:HOH427 3.6 18.4 1.0
OE1 A:GLU106 4.0 4.5 1.0
NE2 A:HIS119 4.1 1.8 1.0
CG A:HIS96 4.1 3.1 1.0
CD2 A:HIS119 4.2 3.1 1.0
CG A:HIS94 4.2 5.5 1.0
ND1 A:HIS94 4.2 3.2 1.0
ND1 A:HIS96 4.2 5.0 1.0
O A:HOH428 4.3 25.5 1.0
O A:HOH458 4.7 32.3 1.0
CD A:GLU106 4.8 4.1 1.0
CB A:THR199 4.9 4.8 1.0
CA A:HIS119 4.9 3.6 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: Wed Oct 16 23:49:31 2024

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