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Zinc in PDB 4hey: Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure

Enzymatic activity of Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure

All present enzymatic activity of Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure:
4.2.1.1;

Protein crystallography data

The structure of Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure, PDB code: 4hey was solved by M.Aggarwal, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.418, 41.334, 71.958, 90.00, 104.44, 90.00
R / Rfree (%) 14.3 / 18.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure (pdb code 4hey). 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 Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure, PDB code: 4hey:

Zinc binding site 1 out of 1 in 4hey

Go back to Zinc Binding Sites List in 4hey
Zinc binding site 1 out of 1 in the Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Activity Enhancers of H64A Variant of Human Carbonic Anhydrase II Possess Multiple Binding Sites Within and Around the Enzyme Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:5.2
occ:1.00
 NE2 A:HIS96 2.0 3.9 1.0
NE2 A:HIS94 2.0 3.8 1.0
ND1 A:4MZ303 2.0 7.5 0.9
ND1 A:HIS119 2.1 4.3 1.0
CE1 A:HIS119 2.9 3.8 1.0
CD2 A:HIS94 3.0 5.0 1.0
CE1 A:4MZ303 3.0 9.5 0.9
CE1 A:HIS96 3.0 4.7 1.0
CD2 A:HIS96 3.0 4.2 1.0
CE1 A:HIS94 3.0 4.3 1.0
HE1 A:HIS119 3.0 4.5 1.0
CG A:4MZ303 3.1 9.3 0.9
HD2 A:HIS94 3.1 6.0 1.0
CG A:HIS119 3.1 3.3 1.0
HD2 A:HIS96 3.2 5.0 1.0
HE1 A:HIS96 3.2 5.6 1.0
HB2 A:HIS119 3.2 5.1 1.0
HE1 A:HIS94 3.2 5.2 1.0
HG1 A:THR199 3.4 6.0 1.0
C4 A:4MZ303 3.5 12.0 0.9
CB A:HIS119 3.6 4.3 1.0
HB3 A:HIS119 3.8 5.1 1.0
OG1 A:THR199 3.8 5.0 1.0
OE1 A:GLU106 4.0 5.7 1.0
NE2 A:HIS119 4.1 5.3 1.0
ND1 A:HIS96 4.1 5.4 1.0
ND1 A:HIS94 4.1 4.7 1.0
CG A:HIS94 4.1 5.0 1.0
CG A:HIS96 4.1 5.2 1.0
NE2 A:4MZ303 4.1 10.7 0.9
CD2 A:4MZ303 4.2 9.3 0.9
CD2 A:HIS119 4.2 4.7 1.0
HH2 A:TRP209 4.4 6.3 1.0
O A:HOH434 4.4 15.0 1.0
HE2 A:HIS119 4.8 6.4 1.0
CD A:GLU106 4.9 5.7 1.0
HD1 A:HIS96 4.9 6.5 1.0
HD1 A:HIS94 4.9 5.7 1.0

Reference:

M.Aggarwal, B.Kondeti, C.Tu, C.M.Maupin, D.N.Silverman, R.Mckenna. Structural Insight Into Activity Enhancement and Inhibition of H64A Carbonic Anhydrase II By Imidazoles. Iucrj V. 1 129 2014.
ISSN: ESSN 2052-2525
PubMed: 25075329
DOI: 10.1107/S2052252514004096
Page generated: Sun Oct 27 00:04:13 2024

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