Zinc in PDB 3e1v: H. Influenzae Beta-Carbonic Anhydrase, Variant D44N

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant D44N:
4.2.1.1;

The structure of H. Influenzae Beta-Carbonic Anhydrase, Variant D44N, PDB code: 3e1v was solved by R.S.Rowlett, D.A.Chapnick, S.Shah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.84 / 2.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.574, 81.574, 187.846, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.3

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant D44N (pdb code 3e1v). 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 D44N, PDB code: 3e1v:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant D44N


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 D44N within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn230 b:36.3 occ:1.00 NE2 A:HIS98 2.1 35.2 1.0 SG A:CYS101 2.3 35.3 1.0 SG A:CYS42 2.3 39.7 1.0 O A:HOH231 2.6 12.5 1.0 CE1 A:HIS98 2.8 35.0 1.0 CD2 A:HIS98 3.2 34.5 1.0 CB A:CYS101 3.3 34.6 1.0 CB A:CYS42 3.4 40.9 1.0 CA A:CYS101 3.6 34.6 1.0 CB A:ASN44 3.7 42.9 1.0 OD1 A:ASN44 3.7 42.4 1.0 N A:GLY102 3.9 34.1 1.0 ND1 A:HIS98 4.0 34.0 1.0 CG A:ASN44 4.1 42.2 1.0 C A:CYS101 4.1 34.4 1.0 CG A:HIS98 4.2 34.2 1.0 N A:GLY103 4.5 34.7 1.0 N A:ALA67 4.7 34.4 1.0 CA A:ALA67 4.8 34.4 1.0 CA A:CYS42 4.8 40.8 1.0 N A:ASN44 4.8 42.4 1.0 CA A:ASN44 4.9 42.8 1.0 N A:CYS101 4.9 34.9 1.0 CA A:GLY102 5.0 34.4 1.0

Zinc binding site 2 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant D44N


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 D44N within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn230 b:37.3 occ:1.00 NE2 B:HIS98 2.1 35.2 1.0 SG B:CYS101 2.3 30.1 1.0 SG B:CYS42 2.3 39.6 1.0 CE1 B:HIS98 3.0 33.9 1.0 O B:HOH231 3.0 14.6 1.0 CD2 B:HIS98 3.2 33.9 1.0 CB B:CYS101 3.2 30.2 1.0 CA B:CYS101 3.5 29.9 1.0 CB B:CYS42 3.5 41.8 1.0 CB B:ASN44 3.7 51.9 1.0 N B:GLY102 3.9 29.8 1.0 C B:CYS101 4.0 29.6 1.0 ND1 B:HIS98 4.1 32.8 1.0 CG B:HIS98 4.2 32.7 1.0 N B:GLY103 4.3 30.8 1.0 CG B:ASN44 4.4 53.0 1.0 N B:ALA67 4.7 32.4 1.0 ND2 B:ASN44 4.8 54.0 1.0 N B:CYS101 4.8 30.5 1.0 N B:ASN44 4.8 50.0 1.0 CA B:ALA67 4.8 33.1 1.0 CA B:ASN44 4.9 51.8 1.0 CA B:CYS42 4.9 42.2 1.0 O B:CYS101 4.9 28.0 1.0 CA B:GLY102 5.0 30.1 1.0

R.S.Rowlett, C.Tu, J.Lee, A.G.Herman, D.A.Chapnick, S.H.Shah, P.C.Gareiss. Allosteric Site Variants of Haemophilus Influenzae Beta-Carbonic Anhydrase. Biochemistry V. 48 6146 2009.
ISSN: ISSN 0006-2960
PubMed: 19459702
DOI: 10.1021/BI900663H