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Zinc in PDB 4xz5: Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium

Enzymatic activity of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium

All present enzymatic activity of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium:
4.2.1.1;

Protein crystallography data

The structure of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium, PDB code: 4xz5 was solved by B.P.Mahon, N.A.Diaz-Torres, M.A.Pinard, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 127.059, 102.228, 105.021, 90.00, 127.26, 90.00
R / Rfree (%) 17.1 / 24

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium (pdb code 4xz5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium, PDB code: 4xz5:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4xz5

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Zinc binding site 1 out of 4 in the Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:25.1
occ:1.00
 O3 A:BCT402 2.0 33.8 1.0
ND1 A:HIS184 2.0 22.4 1.0
NE2 A:HIS165 2.1 28.1 1.0
NE2 A:HIS167 2.1 25.7 1.0
CE1 A:HIS184 2.9 27.0 1.0
CD2 A:HIS165 3.0 27.8 1.0
CE1 A:HIS165 3.0 25.1 1.0
CG A:HIS184 3.1 18.2 1.0
CE1 A:HIS167 3.1 21.1 1.0
C A:BCT402 3.1 34.8 1.0
CD2 A:HIS167 3.1 26.4 1.0
O2 A:BCT402 3.3 27.2 1.0
CB A:HIS184 3.5 6.8 1.0
OG1 A:THR252 3.8 25.3 1.0
OE1 A:GLU171 3.9 36.4 1.0
NE2 A:HIS184 4.1 24.2 1.0
ND1 A:HIS165 4.1 22.4 1.0
O1 A:BCT402 4.1 42.3 1.0
CG A:HIS165 4.1 21.6 1.0
CD2 A:HIS184 4.2 16.3 1.0
ND1 A:HIS167 4.2 25.2 1.0
CG A:HIS167 4.3 23.5 1.0
O A:HOH505 4.5 18.1 1.0
CD A:GLU171 4.9 35.9 1.0
CA A:HIS184 4.9 13.1 1.0

Zinc binding site 2 out of 4 in 4xz5

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Zinc binding site 2 out of 4 in the Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:24.8
occ:1.00
 ND1 B:HIS184 2.0 13.6 1.0
NE2 B:HIS165 2.0 24.5 1.0
O2 B:BCT402 2.1 34.5 1.0
NE2 B:HIS167 2.1 34.4 1.0
CE1 B:HIS184 2.8 13.5 1.0
C B:BCT402 2.9 31.9 1.0
O3 B:BCT402 2.9 28.1 1.0
CD2 B:HIS165 3.0 24.7 1.0
CE1 B:HIS165 3.0 22.8 1.0
CD2 B:HIS167 3.1 26.9 1.0
CE1 B:HIS167 3.1 4.1 1.0
CG B:HIS184 3.2 16.4 1.0
OG1 B:THR252 3.6 30.6 1.0
CB B:HIS184 3.7 9.3 1.0
OE1 B:GLU171 3.9 28.7 1.0
NE2 B:HIS184 4.0 14.2 1.0
O1 B:BCT402 4.0 37.3 1.0
ND1 B:HIS165 4.1 26.1 1.0
CG B:HIS165 4.1 25.9 1.0
CD2 B:HIS184 4.2 16.4 1.0
CG B:HIS167 4.2 25.6 1.0
ND1 B:HIS167 4.2 23.4 1.0
CD B:GLU171 4.9 25.3 1.0
CB B:THR252 5.0 15.1 1.0

Zinc binding site 3 out of 4 in 4xz5

Go back to Zinc Binding Sites List in 4xz5
Zinc binding site 3 out of 4 in the Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:26.5
occ:1.00
 ND1 C:HIS184 2.0 25.6 1.0
NE2 C:HIS165 2.0 30.6 1.0
NE2 C:HIS167 2.0 17.6 1.0
O1 C:BCT402 2.1 38.2 1.0
C C:BCT402 2.8 24.1 1.0
CE1 C:HIS184 2.8 26.8 1.0
CD2 C:HIS165 2.9 27.0 1.0
O2 C:BCT402 3.0 29.4 1.0
CE1 C:HIS167 3.0 13.9 1.0
CE1 C:HIS165 3.0 23.7 1.0
CD2 C:HIS167 3.1 24.8 1.0
CG C:HIS184 3.1 28.3 1.0
CB C:HIS184 3.6 23.4 1.0
OG1 C:THR252 3.8 29.2 1.0
OE1 C:GLU171 3.9 32.9 1.0
O3 C:BCT402 3.9 24.4 1.0
NE2 C:HIS184 4.0 29.5 1.0
CG C:HIS165 4.1 26.1 1.0
ND1 C:HIS165 4.1 24.1 1.0
ND1 C:HIS167 4.1 18.7 1.0
CD2 C:HIS184 4.1 29.4 1.0
CG C:HIS167 4.2 28.6 1.0
CD C:GLU171 4.9 38.6 1.0

Zinc binding site 4 out of 4 in 4xz5

Go back to Zinc Binding Sites List in 4xz5
Zinc binding site 4 out of 4 in the Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of the Thermostable Alpha-Carbonic Anydrase From Thiomicrospira Crunogena Xcl-2 Gammaproteobacterium within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn401

b:24.2
occ:1.00
 O2 D:BCT402 1.9 25.2 1.0
NE2 D:HIS165 2.0 36.9 1.0
ND1 D:HIS184 2.1 24.2 1.0
NE2 D:HIS167 2.2 23.7 1.0
C D:BCT402 2.8 20.4 1.0
CD2 D:HIS165 2.9 27.3 1.0
O3 D:BCT402 3.0 19.4 1.0
CE1 D:HIS184 3.0 25.1 1.0
CE1 D:HIS165 3.0 32.7 1.0
CD2 D:HIS167 3.0 26.0 1.0
CG D:HIS184 3.2 22.0 1.0
CE1 D:HIS167 3.2 21.4 1.0
CB D:HIS184 3.6 15.7 1.0
OG1 D:THR252 3.7 25.0 1.0
O1 D:BCT402 3.9 28.9 1.0
OE1 D:GLU171 4.0 25.1 1.0
CG D:HIS165 4.1 22.4 1.0
ND1 D:HIS165 4.1 22.0 1.0
NE2 D:HIS184 4.1 26.8 1.0
CG D:HIS167 4.2 29.5 1.0
ND1 D:HIS167 4.3 25.5 1.0
CD2 D:HIS184 4.3 23.5 1.0
CD D:GLU171 4.9 32.2 1.0

Reference:

N.A.Diaz-Torres, B.P.Mahon, C.D.Boone, M.A.Pinard, C.Tu, R.Ng, M.Agbandje-Mckenna, D.Silverman, K.Scott, R.Mckenna. Structural and Biophysical Characterization of the Alpha-Carbonic Anhydrase From the Gammaproteobacterium Thiomicrospira Crunogena Xcl-2: Insights Into Engineering Thermostable Enzymes For CO2 Sequestration. Acta Crystallogr.,Sect.D V. 71 1745 2015.
ISSN: ESSN 1399-0047
PubMed: 26249355
DOI: 10.1107/S1399004715012183
Page generated: Sun Oct 27 10:54:07 2024

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