Zinc in PDB 3pbm: The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa

All present enzymatic activity of The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa:
3.5.4.4;

The structure of The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa, PDB code: 3pbm was solved by Z.Zhang, S.K.Burley, S.Swaminathan, New York Sgx Research Center Forstructural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.35 / 2.59
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.685, 74.103, 178.215, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 23.2

The structure of The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa (pdb code 3pbm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa, PDB code: 3pbm:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn327 b:24.1 occ:1.00 NE2 A:HIS16 2.1 19.7 1.0 NE2 A:HIS18 2.2 18.9 1.0 NE2 A:HIS196 2.3 18.1 1.0 OD1 A:ASP277 2.4 21.8 1.0 CL01 A:ES4328 2.4 31.1 1.0 CD2 A:HIS18 3.0 16.7 1.0 CE1 A:HIS196 3.0 16.8 1.0 CD2 A:HIS16 3.0 19.4 1.0 CE1 A:HIS16 3.2 17.3 1.0 CG A:ASP277 3.2 21.0 1.0 C02 A:ES4328 3.2 20.1 1.0 CE1 A:HIS18 3.3 17.1 1.0 CD2 A:HIS196 3.3 16.3 1.0 N09 A:ES4328 3.5 18.5 1.0 C10 A:ES4328 3.5 18.0 1.0 OD2 A:ASP277 3.6 23.4 1.0 NE2 A:HIS220 3.8 19.4 1.0 ND1 A:HIS196 4.2 15.5 1.0 CG A:HIS18 4.2 17.0 1.0 CG A:HIS16 4.2 19.6 1.0 N03 A:ES4328 4.2 20.1 1.0 ND1 A:HIS16 4.3 22.0 1.0 ND1 A:HIS18 4.3 18.2 1.0 CD2 A:HIS220 4.3 18.4 1.0 CG A:HIS196 4.4 15.4 1.0 CB A:ASP277 4.4 16.7 1.0 OD2 A:ASP278 4.4 16.8 1.0 C08 A:ES4328 4.7 19.5 1.0 CE1 A:HIS220 4.7 22.6 1.0 C06 A:ES4328 4.7 17.5 1.0 CE2 A:PHE98 4.8 17.1 1.0 CA A:ASP277 4.8 17.4 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn327 b:26.7 occ:1.00 OD1 B:ASP277 2.2 19.8 1.0 NE2 B:HIS18 2.2 19.1 1.0 NE2 B:HIS16 2.3 17.3 1.0 NE2 B:HIS196 2.4 17.4 1.0 CL01 B:ES4328 2.5 42.4 1.0 CD2 B:HIS18 3.0 18.8 1.0 CG B:ASP277 3.1 20.0 1.0 C02 B:ES4328 3.2 23.1 1.0 CD2 B:HIS16 3.2 16.4 1.0 CD2 B:HIS196 3.3 18.6 1.0 CE1 B:HIS16 3.3 21.0 1.0 CE1 B:HIS18 3.4 20.2 1.0 CE1 B:HIS196 3.4 15.7 1.0 OD2 B:ASP277 3.4 24.3 1.0 C10 B:ES4328 3.5 21.0 1.0 N09 B:ES4328 3.5 21.0 1.0 NE2 B:HIS220 3.7 22.4 1.0 N03 B:ES4328 4.1 22.2 1.0 CG B:HIS18 4.3 21.1 1.0 OD2 B:ASP278 4.3 20.9 1.0 CD2 B:HIS220 4.3 22.6 1.0 ND1 B:HIS18 4.4 18.6 1.0 CG B:HIS16 4.4 20.2 1.0 ND1 B:HIS16 4.4 17.6 1.0 ND1 B:HIS196 4.5 17.7 1.0 CG B:HIS196 4.5 19.2 1.0 CB B:ASP277 4.5 20.2 1.0 C06 B:ES4328 4.6 20.8 1.0 CE1 B:HIS220 4.7 22.6 1.0 C08 B:ES4328 4.8 20.2 1.0 CE2 B:PHE98 4.8 18.7 1.0 CA B:ASP277 4.8 18.5 1.0 O B:ASP277 4.8 19.8 1.0

Z.Zhang, S.K.Burley, S.Swaminathan. The Crystal Structure of Adenosine Deaminase in Complex with Chloropurine From Pseudomonas Aeruginosa To Be Published.