Zinc in PDB 3e3f: H. Influenzae Beta-Carbonic Anhydrase, Variant V47A with 100 Mm Bicarbonate

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant V47A with 100 Mm Bicarbonate:
4.2.1.1;

The structure of H. Influenzae Beta-Carbonic Anhydrase, Variant V47A with 100 Mm Bicarbonate, PDB code: 3e3f was solved by R.S.Rowlett, M.Mysliwiec, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.93 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	83.897, 83.897, 184.867, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 23

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A with 100 Mm Bicarbonate (pdb code 3e3f). 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 with 100 Mm Bicarbonate, PDB code: 3e3f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A with 100 Mm Bicarbonate


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 with 100 Mm Bicarbonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn230 b:43.9 occ:1.00 NE2 A:HIS98 1.9 38.3 1.0 SG A:CYS42 2.2 43.6 1.0 SG A:CYS101 2.3 40.0 1.0 OD2 A:ASP44 2.5 49.0 1.0 CE1 A:HIS98 2.8 36.6 1.0 CD2 A:HIS98 2.9 36.7 1.0 CB A:ASP44 3.1 49.7 1.0 CG A:ASP44 3.2 48.4 1.0 CB A:CYS101 3.2 40.0 1.0 CB A:CYS42 3.3 45.0 1.0 CA A:CYS101 3.7 39.9 1.0 ND1 A:HIS98 3.9 34.2 1.0 CG A:HIS98 4.0 37.2 1.0 N A:GLY102 4.1 40.7 1.0 C A:CYS101 4.2 40.3 1.0 CA A:ASP44 4.3 49.6 1.0 N A:ASP44 4.3 48.1 1.0 N A:SER45 4.3 52.6 1.0 O A:HOH242 4.3 29.7 1.0 OD1 A:ASP44 4.4 50.7 1.0 N A:GLY103 4.5 42.0 1.0 CA A:CYS42 4.7 44.9 1.0 N A:ALA67 4.8 44.2 1.0 C A:ASP44 4.8 51.0 1.0 CA A:ALA67 4.9 43.7 1.0 CA A:SER45 5.0 53.7 1.0 N A:CYS101 5.0 39.7 1.0 C A:CYS42 5.0 45.1 1.0 OD1 A:ASN68 5.0 46.2 1.0

Zinc binding site 2 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A with 100 Mm Bicarbonate


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 with 100 Mm Bicarbonate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn230 b:39.4 occ:1.00 SG B:CYS101 1.9 35.0 1.0 NE2 B:HIS98 2.3 45.5 1.0 OD2 B:ASP44 2.3 43.5 1.0 SG B:CYS42 2.3 41.7 1.0 CG B:ASP44 3.0 43.8 1.0 CE1 B:HIS98 3.1 40.6 1.0 CB B:ASP44 3.1 46.5 1.0 CB B:CYS101 3.2 40.7 1.0 CB B:CYS42 3.2 42.8 1.0 CD2 B:HIS98 3.3 43.4 1.0 CA B:CYS101 3.6 40.4 1.0 OD1 B:ASP44 4.0 42.9 1.0 N B:ASP44 4.2 45.3 1.0 ND1 B:HIS98 4.2 44.5 1.0 CA B:ASP44 4.2 47.1 1.0 N B:GLY102 4.3 41.5 1.0 CG B:HIS98 4.3 45.4 1.0 C B:CYS101 4.4 40.8 1.0 O B:HOH237 4.6 31.9 1.0 CA B:CYS42 4.6 43.9 1.0 N B:ALA67 4.8 48.0 1.0 N B:CYS101 4.8 41.8 1.0 N B:GLY103 4.9 43.6 1.0 CA B:ALA67 5.0 47.5 1.0 C B:CYS42 5.0 44.0 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