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Zinc in PDB 4x5s: The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense.

Enzymatic activity of The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense.

All present enzymatic activity of The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense.:
4.2.1.1;

Protein crystallography data

The structure of The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense., PDB code: 4x5s was solved by G.De Simone, V.Alterio, A.Di Fiore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.470, 89.430, 114.820, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 21.5

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense. (pdb code 4x5s). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense., PDB code: 4x5s:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4x5s

Go back to Zinc Binding Sites List in 4x5s
Zinc binding site 1 out of 2 in the The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:13.9
occ:1.00
NE2 A:HIS89 2.0 9.8 1.0
N1 A:AZM302 2.0 10.6 1.0
NE2 A:HIS91 2.0 13.2 1.0
ND1 A:HIS108 2.1 9.2 1.0
CD2 A:HIS89 2.9 9.2 1.0
CD2 A:HIS91 2.9 14.1 1.0
CE1 A:HIS89 3.0 12.1 1.0
CE1 A:HIS108 3.0 10.2 1.0
O2 A:AZM302 3.1 11.6 1.0
S1 A:AZM302 3.1 14.4 1.0
CE1 A:HIS91 3.1 13.0 1.0
CG A:HIS108 3.2 12.0 1.0
CB A:HIS108 3.6 10.7 1.0
OE1 A:GLU95 3.8 16.8 1.0
OG1 A:THR174 4.0 9.5 1.0
CG A:HIS89 4.1 9.7 1.0
ND1 A:HIS89 4.1 10.7 1.0
CG A:HIS91 4.1 14.0 1.0
O1 A:AZM302 4.2 14.3 1.0
ND1 A:HIS91 4.2 13.7 1.0
NE2 A:HIS108 4.2 9.8 1.0
C1 A:AZM302 4.2 15.5 1.0
CD2 A:HIS108 4.3 10.1 1.0
CD A:GLU95 4.8 14.5 1.0
N3 A:AZM302 4.9 16.8 1.0

Zinc binding site 2 out of 2 in 4x5s

Go back to Zinc Binding Sites List in 4x5s
Zinc binding site 2 out of 2 in the The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of An Alpha Carbonic Anhydrase From the Extremophilic Bacterium Sulfurihydrogenibium Azorense. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:13.7
occ:1.00
NE2 B:HIS89 2.0 10.9 1.0
N1 B:AZM302 2.0 13.3 1.0
NE2 B:HIS91 2.0 12.0 1.0
ND1 B:HIS108 2.2 8.3 1.0
CD2 B:HIS89 2.9 12.2 1.0
CD2 B:HIS91 2.9 10.7 1.0
CE1 B:HIS89 3.0 12.1 1.0
CE1 B:HIS108 3.0 9.5 1.0
S1 B:AZM302 3.1 14.8 1.0
O2 B:AZM302 3.1 11.4 1.0
CE1 B:HIS91 3.1 13.4 1.0
CG B:HIS108 3.2 10.1 1.0
CB B:HIS108 3.6 11.3 1.0
OE1 B:GLU95 3.8 14.4 1.0
OG1 B:THR174 4.0 11.7 1.0
CG B:HIS89 4.0 11.6 1.0
ND1 B:HIS89 4.1 10.9 1.0
CG B:HIS91 4.1 12.8 1.0
O1 B:AZM302 4.1 14.1 1.0
ND1 B:HIS91 4.2 12.7 1.0
NE2 B:HIS108 4.2 10.5 1.0
C1 B:AZM302 4.2 14.5 1.0
CD2 B:HIS108 4.3 7.6 1.0
CD B:GLU95 4.7 13.5 1.0
N3 B:AZM302 4.9 17.1 1.0

Reference:

G.De Simone, S.M.Monti, V.Alterio, M.Buonanno, V.De Luca, M.Rossi, V.Carginale, C.T.Supuran, C.Capasso, A.Di Fiore. Crystal Structure of the Most Catalytically Effective Carbonic Anhydrase Enzyme Known, Sazca From the Thermophilic Bacterium Sulfurihydrogenibium Azorense. Bioorg.Med.Chem.Lett. V. 25 2002 2015.
ISSN: ESSN 1464-3405
PubMed: 25817590
DOI: 10.1016/J.BMCL.2015.02.068
Page generated: Wed Dec 16 05:52:49 2020

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