Zinc in PDB 7rtg: Crystal Structure of the Human Adenosine Deaminase 1

All present enzymatic activity of Crystal Structure of the Human Adenosine Deaminase 1:
3.5.4.4;

The structure of Crystal Structure of the Human Adenosine Deaminase 1, PDB code: 7rtg was solved by M.T.Ma, R.L.Lieberman, J.Blazeck, M.R.Jennings, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.17 / 2.59
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.91, 49.519, 89.085, 90, 96.18, 90
R / Rfree (%)	20.1 / 26.1

The binding sites of Zinc atom in the Crystal Structure of the Human Adenosine Deaminase 1 (pdb code 7rtg). 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 of the Human Adenosine Deaminase 1, PDB code: 7rtg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Human Adenosine Deaminase 1


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 the Human Adenosine Deaminase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:39.1 occ:1.00 NE2 A:HIS15 2.0 33.2 1.0 NE2 A:HIS17 2.1 38.6 1.0 NE2 A:HIS214 2.1 38.0 1.0 OD1 A:ASP295 2.1 47.9 1.0 O A:HOH502 2.5 41.7 1.0 CE1 A:HIS15 2.9 35.9 1.0 CE1 A:HIS17 3.0 39.8 1.0 CE1 A:HIS214 3.0 36.9 1.0 CD2 A:HIS15 3.1 34.1 1.0 CD2 A:HIS17 3.1 41.5 1.0 CG A:ASP295 3.2 40.2 1.0 CD2 A:HIS214 3.2 38.7 1.0 CE1 A:HIS238 3.2 43.8 1.0 OD2 A:ASP295 3.5 41.5 1.0 NE2 A:HIS238 3.8 45.2 1.0 ND1 A:HIS15 4.0 35.5 1.0 CG A:HIS15 4.1 32.6 1.0 ND1 A:HIS17 4.1 37.1 1.0 ND1 A:HIS214 4.2 32.6 1.0 CG A:HIS17 4.2 42.6 1.0 ND1 A:HIS238 4.3 40.7 1.0 CG A:HIS214 4.3 31.8 1.0 CB A:ASP295 4.6 38.5 1.0 CA A:ASP295 4.9 37.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Human Adenosine Deaminase 1


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 the Human Adenosine Deaminase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:39.8 occ:1.00 OD1 B:ASP295 2.0 43.8 1.0 NE2 B:HIS214 2.0 36.0 1.0 NE2 B:HIS15 2.0 42.9 1.0 NE2 B:HIS17 2.0 36.0 1.0 O B:HOH503 2.3 42.9 1.0 CE1 B:HIS214 2.9 38.4 1.0 CE1 B:HIS15 2.9 43.2 1.0 CE1 B:HIS17 3.0 35.8 1.0 CG B:ASP295 3.1 40.6 1.0 CD2 B:HIS17 3.1 38.0 1.0 CD2 B:HIS15 3.1 41.6 1.0 CD2 B:HIS214 3.1 36.4 1.0 NE2 B:HIS238 3.4 44.5 1.0 OD2 B:ASP295 3.4 40.6 1.0 ND1 B:HIS214 4.1 38.0 1.0 ND1 B:HIS15 4.1 41.5 1.0 ND1 B:HIS17 4.1 29.8 1.0 CG B:HIS15 4.2 41.5 1.0 CG B:HIS17 4.2 38.8 1.0 CG B:HIS214 4.2 35.5 1.0 CE1 B:HIS238 4.3 45.6 1.0 CD2 B:HIS238 4.4 41.7 1.0 CB B:ASP295 4.4 40.5 1.0 NH1 B:ARG101 4.5 41.6 1.0 CA B:ASP295 4.7 47.5 1.0

M.T.Ma, M.R.Jennings, J.Blazeck, R.L.Lieberman. Catalytically Active Holo Homo Sapiens Adenosine Deaminase I Adopts A Closed Conformation. Acta Crystallogr D Struct V. 78 91 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 34981765
DOI: 10.1107/S2059798321011785