Zinc in PDB 3e2x: H. Influenzae Beta-Carbonic Anhydrase, Variant V47A

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant V47A:
4.2.1.1;

The structure of H. Influenzae Beta-Carbonic Anhydrase, Variant V47A, PDB code: 3e2x was solved by R.S.Rowlett, J.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.98 / 2.55
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.141, 133.317, 143.892, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 28.3

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A (pdb code 3e2x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A, PDB code: 3e2x:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of H. Influenzae Beta-Carbonic Anhydrase, Variant V47A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn230 b:43.6 occ:1.00 OD2 A:ASP44 2.0 48.2 1.0 NE2 A:HIS98 2.1 43.5 1.0 SG A:CYS101 2.3 41.6 1.0 SG A:CYS42 2.3 47.9 1.0 CG A:ASP44 2.9 48.6 1.0 CE1 A:HIS98 2.9 43.8 1.0 CD2 A:HIS98 3.1 43.6 1.0 OD1 A:ASP44 3.3 46.5 1.0 CB A:CYS101 3.3 43.0 1.0 CB A:CYS42 3.4 46.8 1.0 CA A:CYS101 3.7 43.2 1.0 ND1 A:HIS98 4.0 43.3 1.0 N A:GLY102 4.1 43.9 1.0 N A:SER45 4.2 52.7 1.0 CG A:HIS98 4.2 43.1 1.0 C A:CYS101 4.2 43.5 1.0 CB A:ASP44 4.2 49.7 1.0 C A:ASP44 4.2 51.1 1.0 N A:ASP44 4.3 49.3 1.0 CA A:ASP44 4.4 50.2 1.0 N A:GLY103 4.5 44.3 1.0 O A:ASP44 4.7 51.4 1.0 CA A:SER45 4.7 53.9 1.0 CA A:CYS42 4.8 47.0 1.0 CB A:SER45 4.9 53.9 1.0 C A:CYS42 5.0 47.5 1.0

Zinc binding site 2 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of H. Influenzae Beta-Carbonic Anhydrase, Variant V47A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn230 b:46.2 occ:1.00 OD2 B:ASP44 2.0 51.3 1.0 NE2 B:HIS98 2.1 42.8 1.0 SG B:CYS101 2.3 41.8 1.0 SG B:CYS42 2.3 47.0 1.0 CG B:ASP44 2.8 50.2 1.0 CE1 B:HIS98 3.0 41.4 1.0 CB B:ASP44 3.0 50.6 1.0 CD2 B:HIS98 3.1 41.5 1.0 CB B:CYS101 3.3 43.3 1.0 CB B:CYS42 3.4 46.7 1.0 CA B:CYS101 3.6 43.8 1.0 OD1 B:ASP44 3.9 50.2 1.0 N B:GLY102 4.1 43.8 1.0 ND1 B:HIS98 4.1 42.6 1.0 CA B:ASP44 4.1 51.0 1.0 C B:CYS101 4.2 43.7 1.0 CG B:HIS98 4.2 42.8 1.0 N B:ASP44 4.2 49.8 1.0 N B:SER45 4.3 53.7 1.0 N B:GLY103 4.5 43.9 1.0 C B:ASP44 4.6 52.0 1.0 CA B:CYS42 4.7 46.7 1.0 N B:CYS101 4.9 43.9 1.0 C B:CYS42 5.0 47.2 1.0

R.S.Rowlett, K.M.Hoffmann, H.Failing, M.M.Mysliwiec, D.Samardzic. Evidence For A Bicarbonate "Escort" Site in Haemophilus Influenzae Beta-Carbonic Anhydrase . Biochemistry V. 49 3640 2010.
ISSN: ISSN 0006-2960
PubMed: 20359198
DOI: 10.1021/BI100328J