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Zinc in PDB 8c0r: Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative.

Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative.

All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative.:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative., PDB code: 8c0r 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) 24.60 / 1.56
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.342, 41.484, 72.053, 90, 104.38, 90
R / Rfree (%) 17.7 / 20.1

Other elements in 8c0r:

The structure of Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative. also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative. (pdb code 8c0r). 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 Human Carbonic Anhydrase II in Complex with A Coumarin Derivative., PDB code: 8c0r:

Zinc binding site 1 out of 1 in 8c0r

Go back to Zinc Binding Sites List in 8c0r
Zinc binding site 1 out of 1 in the Crystal Structure of Human Carbonic Anhydrase II in Complex with A Coumarin Derivative.


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 Human Carbonic Anhydrase II in Complex with A Coumarin Derivative. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:6.0
occ:1.00
 N1 A:SXL302 2.0 7.2 1.0
NE2 A:HIS94 2.0 4.0 1.0
NE2 A:HIS96 2.0 6.5 1.0
ND1 A:HIS119 2.0 4.6 1.0
CE1 A:HIS119 2.9 3.9 1.0
CD2 A:HIS96 3.0 3.9 1.0
CD2 A:HIS94 3.0 5.5 1.0
CE1 A:HIS94 3.1 4.5 1.0
CE1 A:HIS96 3.1 6.4 1.0
CG A:HIS119 3.1 4.3 1.0
S1 A:SXL302 3.2 8.2 1.0
F1 A:SXL302 3.2 14.1 1.0
O1 A:SXL302 3.4 8.6 1.0
CB A:HIS119 3.5 3.4 1.0
C1 A:SXL302 3.8 11.7 1.0
OG1 A:THR199 3.9 4.2 1.0
OE1 A:GLU106 3.9 4.3 1.0
NE2 A:HIS119 4.1 4.3 1.0
CG A:HIS96 4.2 5.3 1.0
CG A:HIS94 4.2 5.0 1.0
ND1 A:HIS94 4.2 5.1 1.0
ND1 A:HIS96 4.2 5.5 1.0
CD2 A:HIS119 4.2 4.7 1.0
F2 A:SXL302 4.3 13.9 1.0
O2 A:SXL302 4.3 10.0 1.0
CD A:GLU106 4.9 7.8 1.0
CH2 A:TRP209 4.9 3.4 1.0

Reference:

E.Langella, D.Esposito, S.M.Monti, C.T.Supuran, G.De Simone, V.Alterio. A Combined in Silico and Structural Study Opens New Perspectives on Aliphatic Sulfonamides, A Still Poorly Investigated Class of Ca Inhibitors. Biology (Basel) V. 12 2023.
ISSN: ESSN 2079-7737
PubMed: 36829558
DOI: 10.3390/BIOLOGY12020281
Page generated: Wed Oct 30 18:33:59 2024

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