Zinc in PDB 1v9e: Crystal Structure Analysis of Bovine Carbonic Anhydrase II

All present enzymatic activity of Crystal Structure Analysis of Bovine Carbonic Anhydrase II:
4.2.1.1;

The structure of Crystal Structure Analysis of Bovine Carbonic Anhydrase II, PDB code: 1v9e was solved by R.Saito, T.Sato, A.Ikai, N.Tanaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.87 / 1.95
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	66.700, 66.700, 240.000, 90.00, 90.00, 120.00
R / Rfree (%)	27 / 29.8

The binding sites of Zinc atom in the Crystal Structure Analysis of Bovine Carbonic Anhydrase II (pdb code 1v9e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure Analysis of Bovine Carbonic Anhydrase II, PDB code: 1v9e:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure Analysis of Bovine Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Bovine Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn260 b:16.6 occ:1.00 NE2 A:HIS93 2.1 16.8 1.0 NE2 A:HIS95 2.2 16.2 1.0 O A:HOH462 2.2 12.8 1.0 CD2 A:HIS118 2.3 13.7 1.0 CD2 A:HIS95 2.9 12.5 1.0 CD2 A:HIS93 2.9 15.5 1.0 CG A:HIS118 3.2 13.2 1.0 CE1 A:HIS93 3.2 14.9 1.0 CE1 A:HIS95 3.3 15.8 1.0 NE2 A:HIS118 3.4 14.3 1.0 OG1 A:THR197 3.5 17.0 1.0 CB A:HIS118 3.5 12.7 1.0 O A:HOH279 3.7 19.9 1.0 OE1 A:GLU105 4.0 13.6 1.0 O A:HOH340 4.1 26.0 1.0 CG A:HIS95 4.1 15.4 1.0 CG A:HIS93 4.1 16.1 1.0 ND1 A:HIS93 4.2 16.4 1.0 ND1 A:HIS95 4.3 14.5 1.0 ND1 A:HIS118 4.3 16.5 1.0 CE1 A:HIS118 4.4 12.7 1.0 O A:HOH307 4.5 20.1 1.0 CB A:THR197 4.8 15.8 1.0 CH2 A:TRP207 4.9 11.9 1.0 O A:HOH493 5.0 36.4 1.0 CD A:GLU105 5.0 13.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure Analysis of Bovine Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure Analysis of Bovine Carbonic Anhydrase II within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn260 b:17.1 occ:1.00 NE2 B:HIS95 2.1 13.5 1.0 NE2 B:HIS93 2.1 15.0 1.0 ND1 B:HIS118 2.2 14.2 1.0 O B:HOH478 2.3 13.9 1.0 CD2 B:HIS95 2.8 10.4 1.0 CD2 B:HIS93 3.0 13.9 1.0 CE1 B:HIS118 3.1 13.5 1.0 CE1 B:HIS93 3.2 13.0 1.0 CG B:HIS118 3.2 12.1 1.0 CE1 B:HIS95 3.3 12.9 1.0 CB B:HIS118 3.5 11.6 1.0 OG1 B:THR197 3.6 14.9 1.0 O B:HOH293 3.7 18.7 1.0 CG B:HIS95 4.1 13.5 1.0 OE1 B:GLU105 4.1 11.8 1.0 CG B:HIS93 4.2 13.8 1.0 ND1 B:HIS93 4.2 14.2 1.0 O B:HOH334 4.3 21.5 1.0 NE2 B:HIS118 4.3 12.8 1.0 ND1 B:HIS95 4.3 13.7 1.0 CD2 B:HIS118 4.3 14.4 1.0 O B:HOH282 4.5 19.8 1.0 CB B:THR197 4.9 15.6 1.0 CH2 B:TRP207 5.0 14.4 1.0

R.Saito, T.Sato, A.Ikai, N.Tanaka. Structure of Bovine Carbonic Anhydrase II at 1.95 A Resolution. Acta Crystallogr.,Sect.D V. 60 792 2004.
ISSN: ISSN 0907-4449
PubMed: 15039588
DOI: 10.1107/S0907444904003166