Zinc in PDB 3e24: H. Influenzae Beta-Carbonic Anhydrase, Variant W39F

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant W39F:
4.2.1.1;

The structure of H. Influenzae Beta-Carbonic Anhydrase, Variant W39F, PDB code: 3e24 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)	29.37 / 2.30
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.173, 129.627, 144.081, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.6

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant W39F (pdb code 3e24). 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 W39F, PDB code: 3e24:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant W39F


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 W39F within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn230 b:37.7 occ:1.00 OD2 A:ASP44 2.0 45.4 1.0 NE2 A:HIS98 2.1 38.0 1.0 SG A:CYS101 2.3 36.1 1.0 SG A:CYS42 2.3 36.2 1.0 CG A:ASP44 2.8 47.1 1.0 CB A:ASP44 2.9 47.7 1.0 CE1 A:HIS98 3.0 35.7 1.0 CD2 A:HIS98 3.1 38.0 1.0 CB A:CYS42 3.3 37.0 1.0 CB A:CYS101 3.3 36.7 1.0 CA A:CYS101 3.7 37.1 1.0 O A:HOH237 4.0 32.6 1.0 OD1 A:ASP44 4.0 49.8 1.0 ND1 A:HIS98 4.1 37.4 1.0 N A:GLY102 4.1 36.8 1.0 CA A:ASP44 4.1 47.6 1.0 C A:CYS101 4.2 37.0 1.0 CG A:HIS98 4.2 37.3 1.0 N A:ASP44 4.3 44.9 1.0 N A:SER45 4.4 52.7 1.0 N A:GLY103 4.5 36.9 1.0 CA A:CYS42 4.7 37.6 1.0 C A:ASP44 4.7 50.0 1.0 N A:ALA67 4.8 34.0 1.0 CA A:ALA67 4.9 34.0 1.0 N A:CYS101 5.0 37.1 1.0 C A:CYS42 5.0 37.9 1.0

Zinc binding site 2 out of 2 in the H. Influenzae Beta-Carbonic Anhydrase, Variant W39F


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 W39F within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn230 b:39.0 occ:1.00 OD1 B:ASP44 2.0 39.4 1.0 NE2 B:HIS98 2.1 39.2 1.0 SG B:CYS101 2.3 37.2 1.0 SG B:CYS42 2.3 36.9 1.0 CG B:ASP44 2.7 40.7 1.0 OD2 B:ASP44 3.0 41.4 1.0 CE1 B:HIS98 3.0 38.0 1.0 CD2 B:HIS98 3.0 38.8 1.0 CB B:CYS42 3.3 37.1 1.0 CB B:CYS101 3.3 38.0 1.0 CA B:CYS101 3.7 38.0 1.0 CB B:ASP44 4.1 41.0 1.0 ND1 B:HIS98 4.1 38.8 1.0 CG B:HIS98 4.1 37.6 1.0 N B:GLY102 4.2 37.6 1.0 C B:CYS101 4.2 37.8 1.0 C B:ASP44 4.2 42.7 1.0 N B:SER45 4.2 44.6 1.0 O B:HOH239 4.2 32.1 1.0 N B:ASP44 4.4 40.4 1.0 CA B:ASP44 4.4 41.6 1.0 N B:GLY103 4.5 38.3 1.0 O B:ASP44 4.6 43.0 1.0 CA B:CYS42 4.7 36.9 1.0 N B:ALA67 4.8 34.5 1.0 O B:HOH263 4.9 48.9 1.0 CA B:SER45 4.9 46.0 1.0 CA B:ALA67 4.9 34.5 1.0 C B:CYS42 5.0 37.2 1.0 OD1 B:ASN68 5.0 32.7 1.0 N B:CYS101 5.0 38.2 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