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Zinc in PDB 3t5z: Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide

Enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide

All present enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide, PDB code: 3t5z was solved by A.Di Fiore, A.Maresca, V.Alterio, C.T.Supuran, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.110, 41.320, 71.840, 90.00, 104.32, 90.00
R / Rfree (%) 17.9 / 21.1

Other elements in 3t5z:

The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide (pdb code 3t5z). 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 Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide, PDB code: 3t5z:

Zinc binding site 1 out of 1 in 3t5z

Go back to Zinc Binding Sites List in 3t5z
Zinc binding site 1 out of 1 in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human Carbonic Anhydrase II in Complex with N-Methoxy-Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:7.0
occ:1.00
 N1 A:B09263 2.0 15.2 1.0
NE2 A:HIS94 2.0 5.6 1.0
NE2 A:HIS96 2.0 4.2 1.0
ND1 A:HIS119 2.1 4.0 1.0
CD2 A:HIS96 2.9 5.1 1.0
CE1 A:HIS119 2.9 3.0 1.0
CE1 A:HIS94 3.0 6.4 1.0
O3 A:B09263 3.0 19.6 1.0
CD2 A:HIS94 3.0 7.3 1.0
CE1 A:HIS96 3.1 3.0 1.0
O2 A:B09263 3.2 18.9 1.0
CG A:HIS119 3.2 3.6 1.0
S1 A:B09263 3.2 17.3 1.0
CB A:HIS119 3.6 3.2 1.0
C7 A:B09263 3.6 18.4 1.0
OG1 A:THR199 3.7 6.7 1.0
OE1 A:GLU106 4.0 6.2 1.0
ND1 A:HIS94 4.1 6.3 1.0
NE2 A:HIS119 4.1 3.0 1.0
CG A:HIS96 4.1 3.5 1.0
ND1 A:HIS96 4.1 5.3 1.0
CG A:HIS94 4.1 6.6 1.0
O1 A:B09263 4.1 19.2 1.0
CD2 A:HIS119 4.2 3.6 1.0
C1 A:B09263 4.3 19.3 1.0
O A:HOH460 4.5 16.7 1.0
C2 A:B09263 4.9 21.1 1.0
CD A:GLU106 5.0 6.0 1.0
CB A:THR199 5.0 7.3 1.0

Reference:

A.Di Fiore, A.Maresca, V.Alterio, C.T.Supuran, G.De Simone. Carbonic Anhydrase Inhibitors: X-Ray Crystallographic Studies For the Binding of N-Substituted Benzenesulfonamides to Human Isoform II. Chem.Commun.(Camb.) V. 47 11636 2011.
ISSN: ISSN 1359-7345
PubMed: 21952494
DOI: 10.1039/C1CC14575D
Page generated: Sat Oct 26 16:18:50 2024

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