Zinc in PDB 3e31: 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: 3e31 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)	37.72 / 2.95
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	82.277, 82.277, 188.783, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 24.7

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant V47A (pdb code 3e31). 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: 3e31:
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:57.3 occ:1.00 OD2 A:ASP44 2.0 52.9 1.0 NE2 A:HIS98 2.1 43.3 1.0 SG A:CYS101 2.3 42.2 1.0 SG A:CYS42 2.3 40.9 1.0 CE1 A:HIS98 2.8 41.2 1.0 CG A:ASP44 2.8 50.6 1.0 CB A:ASP44 3.0 50.6 1.0 CD2 A:HIS98 3.1 40.5 1.0 CB A:CYS42 3.2 43.9 1.0 CB A:CYS101 3.3 41.4 1.0 CA A:CYS101 3.9 40.7 1.0 ND1 A:HIS98 3.9 41.1 1.0 N A:GLY102 3.9 39.9 1.0 OD1 A:ASP44 4.0 51.4 1.0 CG A:HIS98 4.1 39.0 1.0 C A:CYS101 4.2 40.5 1.0 CA A:ASP44 4.2 50.9 1.0 N A:ASP44 4.3 49.3 1.0 N A:GLY103 4.5 40.1 1.0 CA A:CYS42 4.6 44.1 1.0 N A:ALA67 4.7 27.5 1.0 CA A:ALA67 4.7 27.4 1.0 OD1 A:ASN68 4.9 27.3 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:51.9 occ:1.00 OD2 B:ASP44 2.0 53.9 1.0 NE2 B:HIS98 2.1 41.6 1.0 SG B:CYS101 2.3 32.2 1.0 SG B:CYS42 2.3 41.4 1.0 CE1 B:HIS98 2.7 39.2 1.0 CG B:ASP44 2.8 54.3 1.0 CB B:CYS101 3.1 34.3 1.0 CD2 B:HIS98 3.2 39.7 1.0 CB B:ASP44 3.2 55.0 1.0 CB B:CYS42 3.4 43.3 1.0 CA B:CYS101 3.7 33.6 1.0 N B:GLY102 3.8 32.4 1.0 OD1 B:ASP44 3.8 55.0 1.0 ND1 B:HIS98 3.8 38.4 1.0 C B:CYS101 4.0 33.1 1.0 CG B:HIS98 4.1 37.6 1.0 N B:GLY103 4.2 31.5 1.0 CA B:ASP44 4.5 55.4 1.0 N B:ASP44 4.5 53.4 1.0 CA B:GLY102 4.8 32.0 1.0 N B:ALA67 4.8 26.4 1.0 CA B:CYS42 4.8 43.9 1.0 CA B:ALA67 4.9 26.0 1.0 CA B:GLY103 5.0 30.9 1.0 O B:CYS101 5.0 32.2 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