Zinc in PDB 3ucn: Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide

All present enzymatic activity of Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide:
4.2.1.1;

The structure of Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide, PDB code: 3ucn was solved by S.Huang, T.Hainzl, A.E.Sauer-Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.32 / 2.25
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.651, 75.651, 222.221, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 20

The structure of Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide (pdb code 3ucn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide, PDB code: 3ucn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn228 b:45.7 occ:1.00 N1 A:AZI229 1.8 37.0 1.0 NE2 A:HIS103 2.2 41.5 1.0 SG A:CYS47 2.3 41.8 1.0 SG A:CYS106 2.4 41.9 1.0 N2 A:AZI229 2.9 35.5 1.0 CD2 A:HIS103 3.1 39.0 1.0 CE1 A:HIS103 3.1 38.9 1.0 CB A:CYS47 3.3 38.2 1.0 CB A:CYS106 3.3 41.6 1.0 CA A:CYS106 3.5 43.2 1.0 CB A:ASP49 3.9 42.5 1.0 N3 A:AZI229 3.9 40.6 1.0 N A:GLY107 4.2 41.5 1.0 C A:CYS106 4.2 41.9 1.0 ND1 A:HIS103 4.2 42.2 1.0 CG A:HIS103 4.3 44.0 1.0 O A:HOH272 4.4 39.6 1.0 OD2 A:ASP49 4.4 46.6 1.0 CG A:ASP49 4.5 46.7 1.0 N A:GLY72 4.6 38.1 1.0 N A:ALA108 4.6 45.3 1.0 CA A:CYS47 4.7 38.3 1.0 CB A:ALA108 4.7 45.4 1.0 N A:CYS106 4.7 46.1 1.0 N A:ASP49 4.8 41.6 1.0 CA A:GLY72 4.8 38.2 1.0 CA A:ASP49 4.9 42.5 1.0

Zinc binding site 2 out of 2 in the Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Coccomyxa Beta-Carbonic Anhydrase in Complex with Azide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn228 b:44.0 occ:1.00 N1 A:AZI230 2.1 43.8 1.0 NE2 B:HIS103 2.1 40.9 1.0 SG B:CYS106 2.3 38.1 1.0 SG B:CYS47 2.3 41.1 1.0 N2 A:AZI230 2.9 46.8 1.0 CE1 B:HIS103 3.0 44.6 1.0 CD2 B:HIS103 3.2 42.4 1.0 CB B:CYS47 3.2 37.8 1.0 CB B:CYS106 3.2 40.7 1.0 CA B:CYS106 3.6 40.9 1.0 N3 A:AZI230 3.9 49.5 1.0 CB B:ASP49 3.9 42.8 1.0 N B:GLY107 4.1 40.4 1.0 C B:CYS106 4.1 40.8 1.0 ND1 B:HIS103 4.2 42.4 1.0 CG B:HIS103 4.3 41.6 1.0 O B:HOH256 4.4 32.8 1.0 OD2 B:ASP49 4.4 40.4 1.0 N B:ALA108 4.6 41.5 1.0 N B:GLY72 4.6 35.8 1.0 CB B:ALA108 4.6 43.2 1.0 CG B:ASP49 4.7 43.9 1.0 CA B:CYS47 4.7 39.4 1.0 N B:ASP49 4.8 40.6 1.0 CA B:GLY72 4.9 35.5 1.0 N B:CYS106 4.9 42.2 1.0 CA B:ASP49 4.9 41.9 1.0

S.Huang, T.Hainzl, C.Grundstrom, C.Forsman, G.Samuelsson, A.E.Sauer-Eriksson. Structural Studies of [Beta]-Carbonic Anhydrase From the Green Alga Coccomyxa: Inhibitor Complexes with Anions and Acetazolamide. Plos One V. 6 28458 2011.
ISSN: ESSN 1932-6203
PubMed: 22162771
DOI: 10.1371/JOURNAL.PONE.0028458