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Zinc in PDB 5o07: The Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor

Enzymatic activity of The Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor

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

Protein crystallography data

The structure of The Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor, PDB code: 5o07 was solved by V.Alterio, G.De Simone, D.Esposito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.29 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.250, 41.252, 71.733, 90.00, 104.26, 90.00
R / Rfree (%) 15.7 / 19.5

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor (pdb code 5o07). 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 the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor, PDB code: 5o07:

Zinc binding site 1 out of 1 in 5o07

Go back to Zinc Binding Sites List in 5o07
Zinc binding site 1 out of 1 in the The Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor


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 the Human Carbonic Anhydrase II in Complex with A Nitroimidazole Sulfamate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:7.4
occ:1.00
 NE2 A:HIS94 2.0 5.9 1.0
NE2 A:HIS96 2.0 6.5 1.0
N1 A:1VQ302 2.0 5.8 1.0
ND1 A:HIS119 2.0 5.8 1.0
CE1 A:HIS119 3.0 5.5 1.0
CD2 A:HIS94 3.0 6.1 1.0
CD2 A:HIS96 3.0 5.9 1.0
CE1 A:HIS94 3.0 6.6 1.0
CE1 A:HIS96 3.0 6.4 1.0
O2 A:1VQ302 3.1 7.5 1.0
S1 A:1VQ302 3.1 8.1 1.0
CG A:HIS119 3.1 3.7 1.0
CB A:HIS119 3.5 3.1 1.0
O3 A:1VQ302 3.9 12.7 1.0
OE1 A:GLU106 3.9 5.9 1.0
OG1 A:THR199 4.0 5.6 1.0
ND1 A:HIS94 4.1 5.0 1.0
CG A:HIS94 4.1 4.8 1.0
ND1 A:HIS96 4.1 5.7 1.0
CG A:HIS96 4.1 5.4 1.0
NE2 A:HIS119 4.2 4.5 1.0
O A:HOH608 4.2 18.7 1.0
CD2 A:HIS119 4.2 3.8 1.0
O1 A:1VQ302 4.2 8.7 1.0
C1 A:1VQ302 4.4 15.1 1.0
CD A:GLU106 4.9 6.7 1.0

Reference:

G.De Simone, E.Langella, D.Esposito, C.T.Supuran, S.M.Monti, J.Y.Winum, V.Alterio. Insights Into the Binding Mode of Sulphamates and Sulphamides to Hca II: Crystallographic Studies and Binding Free Energy Calculations. J Enzyme Inhib Med Chem V. 32 1002 2017.
ISSN: ESSN 1475-6374
PubMed: 28738704
DOI: 10.1080/14756366.2017.1349764
Page generated: Sun Oct 27 23:10:22 2024

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