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Zinc in PDB 1cao: Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions

Enzymatic activity of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions

All present enzymatic activity of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions:
4.2.1.1;

Protein crystallography data

The structure of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions, PDB code: 1cao was solved by S.Mangani, K.Hakansson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions (pdb code 1cao). 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 Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions, PDB code: 1cao:

Zinc binding site 1 out of 1 in 1cao

Go back to Zinc Binding Sites List in 1cao
Zinc binding site 1 out of 1 in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:9.3
occ:1.00
 ND1 A:HIS119 2.1 6.4 1.0
S A:H2S263 2.1 25.4 1.0
NE2 A:HIS96 2.1 3.0 1.0
NE2 A:HIS94 2.1 6.7 1.0
CE1 A:HIS119 2.9 5.0 1.0
CD2 A:HIS94 3.0 7.0 1.0
CD2 A:HIS96 3.0 3.0 1.0
CE1 A:HIS96 3.1 3.2 1.0
CE1 A:HIS94 3.1 8.8 1.0
CG A:HIS119 3.2 6.6 1.0
CB A:HIS119 3.7 3.9 1.0
O A:HOH318 3.8 20.0 1.0
OG1 A:THR199 3.9 3.0 1.0
OE1 A:GLU106 4.0 5.8 1.0
NE2 A:HIS119 4.1 3.0 1.0
O A:HOH292 4.1 19.3 1.0
O A:HOH338 4.2 29.7 1.0
ND1 A:HIS96 4.2 4.8 1.0
CG A:HIS96 4.2 3.0 1.0
CG A:HIS94 4.2 5.2 1.0
CD2 A:HIS119 4.2 6.2 1.0
ND1 A:HIS94 4.2 4.1 1.0
O A:HOH389 4.5 55.9 1.0
CD A:GLU106 4.9 6.8 1.0

Reference:

S.Mangani, K.Hakansson. Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions. Eur.J.Biochem. V. 210 867 1992.
ISSN: ISSN 0014-2956
PubMed: 1336460
DOI: 10.1111/J.1432-1033.1992.TB17490.X
Page generated: Wed Dec 16 02:46:24 2020

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