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Zinc in PDB 4hba: Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond

Enzymatic activity of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond

All present enzymatic activity of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond:
4.2.1.1;

Protein crystallography data

The structure of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond, PDB code: 4hba 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) 19.91 / 1.76
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.284, 41.156, 71.610, 90.00, 104.17, 90.00
R / Rfree (%) 15 / 18.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond (pdb code 4hba). 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 Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond, PDB code: 4hba:

Zinc binding site 1 out of 1 in 4hba

Go back to Zinc Binding Sites List in 4hba
Zinc binding site 1 out of 1 in the Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:14.6
occ:1.00
 O A:HOH409 1.9 12.1 1.0
NE2 A:HIS94 2.0 9.2 1.0
NE2 A:HIS96 2.0 12.9 1.0
ND1 A:HIS119 2.1 12.1 1.0
CD2 A:HIS94 2.9 13.5 1.0
CE1 A:HIS119 2.9 12.2 1.0
HE1 A:HIS119 3.0 14.6 1.0
CD2 A:HIS96 3.0 11.3 1.0
CE1 A:HIS96 3.0 13.8 1.0
HD2 A:HIS94 3.0 16.2 1.0
CE1 A:HIS94 3.1 12.9 1.0
CG A:HIS119 3.2 11.1 1.0
HD2 A:HIS96 3.2 13.6 1.0
HE1 A:HIS96 3.2 16.5 1.0
HB2 A:HIS119 3.2 11.6 1.0
HE1 A:HIS94 3.3 15.5 1.0
HG1 A:THR199 3.5 15.8 1.0
CB A:HIS119 3.6 9.7 1.0
O A:HOH407 3.8 14.6 1.0
HB3 A:HIS119 3.8 11.6 1.0
OG1 A:THR199 3.8 13.1 1.0
OE1 A:GLU106 4.0 13.2 1.0
NE2 A:HIS119 4.1 9.6 1.0
CG A:HIS94 4.1 8.4 1.0
ND1 A:HIS94 4.1 10.4 1.0
ND1 A:HIS96 4.1 10.1 1.0
CG A:HIS96 4.2 8.9 1.0
O A:HOH524 4.2 23.7 1.0
CD2 A:HIS119 4.2 10.1 1.0
HH2 A:TRP209 4.3 15.0 1.0
O A:HOH457 4.3 19.2 1.0
O A:HOH593 4.7 53.8 1.0
HE2 A:HIS119 4.8 11.5 1.0
CD A:GLU106 4.9 14.2 1.0
O A:HOH566 4.9 27.2 1.0
HD1 A:HIS96 4.9 12.1 1.0
HD1 A:HIS94 4.9 12.5 1.0

Reference:

C.D.Boone, A.Habibzadegan, C.Tu, D.N.Silverman, R.Mckenna. Structural and Catalytic Characterization of A Thermally Stable and Acid-Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond. Acta Crystallogr.,Sect.D V. 69 1414 2013.
ISSN: ISSN 0907-4449
PubMed: 23897465
DOI: 10.1107/S0907444913008743
Page generated: Sat Oct 26 23:59:12 2024

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