Zinc in PDB 1t75: Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase

All present enzymatic activity of Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase:
4.2.1.1;

The structure of Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase, PDB code: 1t75 was solved by V.Oganesyan, S.-H.Kim, R.Kim, J.Jancarik, Berkeley Structural Genomicscenter (Bsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	91.29 / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.447, 110.447, 162.536, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 24.6

The binding sites of Zinc atom in the Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase (pdb code 1t75). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase, PDB code: 1t75:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn221 b:40.6 occ:1.00 OD2 A:ASP44 1.9 28.2 1.0 NE2 A:HIS98 1.9 35.7 1.0 SG A:CYS42 2.3 29.2 1.0 SG A:CYS101 2.3 34.6 1.0 CG A:ASP44 2.8 28.2 1.0 CE1 A:HIS98 2.9 35.8 1.0 CD2 A:HIS98 3.0 34.6 1.0 CB A:ASP44 3.2 29.8 1.0 CB A:CYS42 3.3 28.9 1.0 CB A:CYS101 3.4 33.4 1.0 CA A:CYS101 3.8 33.4 1.0 OD1 A:ASP44 4.0 28.0 1.0 ND1 A:HIS98 4.0 35.4 1.0 CG A:HIS98 4.1 34.2 1.0 N A:ASP44 4.3 30.6 1.0 N A:GLY102 4.3 33.1 1.0 CA A:ASP44 4.4 30.2 1.0 C A:CYS101 4.5 32.9 1.0 N A:ALA67 4.6 25.6 1.0 CA A:ALA67 4.6 25.4 1.0 CA A:CYS42 4.7 28.3 1.0 O A:HOH233 4.8 41.2 1.0 N A:GLY103 4.9 32.9 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn221 b:34.6 occ:1.00 OD2 B:ASP44 2.0 24.8 1.0 NE2 B:HIS98 2.0 25.8 1.0 SG B:CYS101 2.3 24.9 1.0 SG B:CYS42 2.3 21.8 1.0 CG B:ASP44 3.0 25.1 1.0 CE1 B:HIS98 3.0 25.9 1.0 CD2 B:HIS98 3.0 26.5 1.0 CB B:CYS101 3.2 26.4 1.0 CB B:CYS42 3.3 23.9 1.0 CB B:ASP44 3.5 24.9 1.0 CA B:CYS101 3.6 26.1 1.0 OD1 B:ASP44 4.1 25.0 1.0 ND1 B:HIS98 4.1 24.9 1.0 CG B:HIS98 4.2 25.4 1.0 N B:GLY102 4.2 26.3 1.0 O B:HOH225 4.2 30.2 1.0 C B:CYS101 4.3 26.5 1.0 N B:ASP44 4.6 24.6 1.0 CA B:ASP44 4.6 25.1 1.0 CA B:ALA67 4.7 22.5 1.0 N B:ALA67 4.7 22.5 1.0 CA B:CYS42 4.8 23.6 1.0 N B:GLY103 4.8 26.9 1.0 N B:CYS101 4.8 26.2 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn221 b:39.3 occ:1.00 NE2 D:HIS98 1.9 31.2 1.0 OD2 D:ASP44 2.0 22.4 1.0 SG D:CYS42 2.3 27.7 1.0 SG D:CYS101 2.4 25.9 1.0 CE1 D:HIS98 2.8 30.1 1.0 CG D:ASP44 2.9 25.1 1.0 CD2 D:HIS98 3.0 31.2 1.0 CB D:ASP44 3.2 24.9 1.0 CB D:CYS42 3.2 27.0 1.0 CB D:CYS101 3.4 28.3 1.0 CA D:CYS101 3.8 28.5 1.0 O D:HOH226 3.9 32.8 1.0 ND1 D:HIS98 4.0 29.7 1.0 OD1 D:ASP44 4.1 24.2 1.0 CG D:HIS98 4.1 28.5 1.0 N D:GLY102 4.1 28.5 1.0 C D:CYS101 4.3 28.1 1.0 N D:ASP44 4.4 25.3 1.0 CA D:ASP44 4.4 25.4 1.0 N D:GLY103 4.6 28.8 1.0 CA D:CYS42 4.6 26.9 1.0 N D:ALA67 4.7 25.6 1.0 CA D:ALA67 4.8 25.6 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn221 b:32.4 occ:1.00 NE2 E:HIS98 2.0 23.5 1.0 OD2 E:ASP44 2.2 21.6 1.0 SG E:CYS101 2.2 21.8 1.0 SG E:CYS42 2.2 21.3 1.0 CD2 E:HIS98 3.0 24.5 1.0 CE1 E:HIS98 3.0 22.6 1.0 CG E:ASP44 3.0 23.1 1.0 CB E:CYS42 3.2 21.7 1.0 CB E:ASP44 3.3 22.5 1.0 CB E:CYS101 3.3 20.8 1.0 CA E:CYS101 3.7 20.6 1.0 O E:HOH265 4.1 29.2 1.0 ND1 E:HIS98 4.1 22.0 1.0 CG E:HIS98 4.1 21.1 1.0 OD1 E:ASP44 4.2 22.0 1.0 N E:GLY102 4.3 20.5 1.0 C E:CYS101 4.3 20.4 1.0 N E:ASP44 4.4 21.6 1.0 CA E:ASP44 4.4 22.5 1.0 CA E:CYS42 4.6 20.9 1.0 N E:ALA67 4.7 20.5 1.0 CA E:ALA67 4.7 20.0 1.0 N E:GLY103 4.7 21.2 1.0 N E:CYS101 5.0 20.4 1.0

V.Oganesyan, S.-H.Kim, R.Kim, J.Jancarik. Crystal Structure of Escherichia Coli Beta Carbonic Anhydrase To Be Published.