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Zinc in PDB 4pxx: Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II

Enzymatic activity of Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II

All present enzymatic activity of Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II, PDB code: 4pxx was solved by C.D.Boone, A.Habibzadegan, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.41 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.847, 72.560, 74.335, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 22.9

Other elements in 4pxx:

The structure of Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II (pdb code 4pxx). 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 A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II, PDB code: 4pxx:

Zinc binding site 1 out of 1 in 4pxx

Go back to Zinc Binding Sites List in 4pxx
Zinc binding site 1 out of 1 in the Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II


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 A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:8.5
occ:1.00
 NE2 A:HIS96 2.0 0.8 1.0
NE2 A:HIS94 2.0 1.0 1.0
O26 A:CHD302 2.0 5.2 0.8
ND1 A:HIS119 2.1 0.3 1.0
O25 A:CHD302 2.5 8.9 0.8
C24 A:CHD302 2.6 5.9 0.8
CE1 A:HIS119 2.9 0.8 1.0
CD2 A:HIS94 3.0 0.5 1.0
CD2 A:HIS96 3.0 1.7 1.0
HE1 A:HIS119 3.0 1.0 1.0
CE1 A:HIS96 3.0 1.3 1.0
CE1 A:HIS94 3.0 3.1 1.0
HD2 A:HIS94 3.1 0.6 1.0
HD2 A:HIS96 3.1 2.0 1.0
CG A:HIS119 3.2 0.5 1.0
HB2 A:HIS119 3.2 0.8 1.0
HE1 A:HIS96 3.2 1.5 1.0
HE1 A:HIS94 3.3 3.8 1.0
HG1 A:THR199 3.4 3.5 1.0
CB A:HIS119 3.6 0.6 1.0
OG1 A:THR199 3.7 2.9 1.0
HB3 A:HIS119 3.8 0.8 1.0
NE2 A:HIS119 4.1 1.1 1.0
OE1 A:GLU106 4.1 0.7 1.0
C23 A:CHD302 4.1 10.5 0.8
ND1 A:HIS96 4.1 0.8 1.0
CG A:HIS94 4.1 0.9 1.0
ND1 A:HIS94 4.1 1.1 1.0
CG A:HIS96 4.1 1.1 1.0
O A:HOH451 4.2 15.2 1.0
CD2 A:HIS119 4.2 0.4 1.0
HH2 A:TRP209 4.4 3.8 1.0
O A:HOH433 4.6 11.9 1.0
C22 A:CHD302 4.7 11.2 0.8
HG23 A:THR200 4.8 5.1 1.0
HE2 A:HIS119 4.8 1.4 1.0
HD1 A:HIS96 4.9 0.9 1.0
HD1 A:HIS94 4.9 1.3 1.0
CD A:GLU106 4.9 2.1 1.0
H A:THR199 5.0 5.4 1.0

Reference:

C.D.Boone, A.Habibzadegan, R.Mckenna. Crystal Structure of A Highly Thermal Stabilized Variant of Human Carbonic Anhydrase II To Be Published.
Page generated: Wed Dec 16 05:42:07 2020

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