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Zinc in PDB 4fl7: The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide

Enzymatic activity of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide

All present enzymatic activity of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide:
4.2.1.1;

Protein crystallography data

The structure of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide, PDB code: 4fl7 was solved by A.Di Fiore, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.160, 41.500, 71.990, 90.00, 104.39, 90.00
R / Rfree (%) 16.3 / 20.3

Other elements in 4fl7:

The structure of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide (pdb code 4fl7). 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 The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide, PDB code: 4fl7:

Zinc binding site 1 out of 1 in 4fl7

Go back to Zinc Binding Sites List in 4fl7
Zinc binding site 1 out of 1 in the The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Human Carbonic Anhydrase II in Complex with N-(Hydroxy)-Benzamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:7.7
occ:1.00
O2 A:BHO304 2.0 13.0 1.0
ND1 A:HIS119 2.0 4.3 1.0
NE2 A:HIS94 2.1 5.3 1.0
NE2 A:HIS96 2.1 5.9 1.0
O1 A:BHO304 2.1 11.4 1.0
C A:BHO304 2.7 12.0 1.0
N A:BHO304 2.8 13.9 1.0
CE1 A:HIS119 2.9 5.1 1.0
CE1 A:HIS94 3.0 6.7 1.0
CD2 A:HIS96 3.1 6.3 1.0
CD2 A:HIS94 3.1 5.8 1.0
CE1 A:HIS96 3.1 5.9 1.0
CG A:HIS119 3.1 4.2 1.0
CB A:HIS119 3.6 2.6 1.0
OG1 A:THR199 3.7 6.6 1.0
OE1 A:GLU106 4.1 4.0 1.0
NE2 A:HIS119 4.1 4.3 1.0
C1 A:BHO304 4.1 12.9 1.0
ND1 A:HIS94 4.2 4.2 1.0
CG A:HIS94 4.2 5.4 1.0
CG A:HIS96 4.2 4.5 1.0
ND1 A:HIS96 4.2 4.6 1.0
CD2 A:HIS119 4.2 4.1 1.0
C3 A:GOL302 4.4 18.9 1.0
C6 A:BHO304 5.0 12.8 1.0
C2 A:GOL302 5.0 20.6 1.0

Reference:

A.Di Fiore, A.Maresca, C.T.Supuran, G.De Simone. Hydroxamate Represents A Versatile Zinc Binding Group For the Development of New Carbonic Anhydrase Inhibitors. Chem.Commun.(Camb.) V. 48 8838 2012.
ISSN: ISSN 1359-7345
PubMed: 22836518
DOI: 10.1039/C2CC34275H
Page generated: Wed Dec 16 05:17:49 2020

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