Zinc in PDB 6ux1: Carbonic Anhydrase II Complexed with Salicylic Acid

Enzymatic activity of Carbonic Anhydrase II Complexed with Salicylic Acid

All present enzymatic activity of Carbonic Anhydrase II Complexed with Salicylic Acid:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Complexed with Salicylic Acid, PDB code: 6ux1 was solved by J.T.Andring, J.E.Combs, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.55 / 1.36
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.427, 41.304, 72.028, 90.00, 104.23, 90.00
R / Rfree (%) 15.4 / 16.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Carbonic Anhydrase II Complexed with Salicylic Acid (pdb code 6ux1). 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 II Complexed with Salicylic Acid, PDB code: 6ux1:

Zinc binding site 1 out of 1 in 6ux1

Go back to Zinc Binding Sites List in 6ux1
Zinc binding site 1 out of 1 in the Carbonic Anhydrase II Complexed with Salicylic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase II Complexed with Salicylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:12.9
occ:1.00
O A:HOH409 2.0 19.9 1.0
NE2 A:HIS94 2.0 12.0 1.0
NE2 A:HIS96 2.0 12.1 1.0
ND1 A:HIS119 2.1 13.3 1.0
O A:HOH526 2.5 43.8 1.0
CE1 A:HIS119 2.9 12.2 1.0
CD2 A:HIS94 2.9 13.2 1.0
CD2 A:HIS96 3.0 11.4 1.0
CE1 A:HIS94 3.0 13.1 1.0
HE1 A:HIS119 3.0 14.7 1.0
CE1 A:HIS96 3.0 15.4 1.0
HD2 A:HIS94 3.1 15.9 1.0
CG A:HIS119 3.2 11.9 1.0
HD2 A:HIS96 3.2 13.7 1.0
HE1 A:HIS96 3.2 18.5 1.0
HB2 A:HIS119 3.2 14.2 1.0
HE1 A:HIS94 3.2 15.7 1.0
HG1 A:THR199 3.5 16.8 1.0
CB A:HIS119 3.6 11.8 1.0
O1' A:SAL303 3.7 26.9 1.0
HB3 A:HIS119 3.8 14.2 1.0
OG1 A:THR199 3.8 13.9 1.0
OE1 A:GLU106 3.9 13.9 1.0
NE2 A:HIS119 4.1 13.5 1.0
CG A:HIS94 4.1 14.2 1.0
ND1 A:HIS94 4.1 14.4 1.0
ND1 A:HIS96 4.1 13.3 1.0
H32 A:GOL302 4.1 26.1 1.0
CG A:HIS96 4.2 11.3 1.0
H31 A:GOL302 4.2 26.1 1.0
CD2 A:HIS119 4.2 12.3 1.0
HH2 A:TRP209 4.2 16.4 1.0
C1' A:SAL303 4.5 25.7 1.0
C3 A:GOL302 4.7 21.8 1.0
O2' A:SAL303 4.7 22.3 1.0
H2 A:GOL302 4.7 21.1 1.0
CD A:GLU106 4.8 15.5 1.0
HE2 A:HIS119 4.8 16.2 1.0
HD1 A:HIS94 4.9 17.3 1.0
HD1 A:HIS96 4.9 15.9 1.0
HG23 A:THR200 4.9 20.0 1.0

Reference:

J.Andring, J.Combs, R.Mckenna. Aspirin: A Suicide Inhibitor of Carbonic Anhydrase II. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32244293
DOI: 10.3390/BIOM10040527
Page generated: Wed Dec 16 13:00:24 2020

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