Zinc in PDB 9nti: Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme

All present enzymatic activity of Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme:
3.5.4.4;

The structure of Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme, PDB code: 9nti was solved by G.Kaur, J.R.Horton, X.Cheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.21 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.444, 109.268, 173.275, 90, 90, 90
R / Rfree (%)	21.6 / 27.4

The binding sites of Zinc atom in the Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme (pdb code 9nti). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme, PDB code: 9nti:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn604 b:95.0 occ:1.00 NE2 A:HIS119 2.3 79.1 1.0 NE2 A:HIS117 2.3 78.0 1.0 NE2 A:HIS362 2.3 60.7 1.0 OD1 A:ASP447 2.7 81.2 1.0 OD2 A:ASP447 2.9 90.7 1.0 CE1 A:HIS362 3.1 60.7 1.0 CE1 A:HIS119 3.1 76.7 1.0 CG A:ASP447 3.1 87.4 1.0 CE1 A:HIS117 3.2 67.4 1.0 CD2 A:HIS119 3.3 83.1 1.0 CD2 A:HIS117 3.3 77.4 1.0 CD2 A:HIS362 3.4 62.7 1.0 CE1 A:HIS390 3.7 74.0 1.0 ND1 A:HIS119 4.2 82.4 1.0 ND1 A:HIS362 4.2 61.6 1.0 CG A:HIS119 4.3 77.7 1.0 ND1 A:HIS117 4.3 78.7 1.0 CG A:HIS362 4.4 62.4 1.0 CG A:HIS117 4.5 73.0 1.0 NE2 A:HIS390 4.5 68.9 1.0 CB A:ASP447 4.6 70.7 1.0 ND1 A:HIS390 4.7 65.8 1.0

Zinc binding site 2 out of 2 in the Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Chimeric Adenosine Deaminase Growth Factor (Adgf) Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn604 b:96.5 occ:1.00 NE2 B:HIS119 2.3 76.0 1.0 NE2 B:HIS362 2.3 71.0 1.0 NE2 B:HIS117 2.3 72.7 1.0 OD1 B:ASP447 2.4 80.9 1.0 CE1 B:HIS117 3.1 81.2 1.0 CD2 B:HIS119 3.2 76.9 1.0 CE1 B:HIS362 3.2 65.4 1.0 CD2 B:HIS362 3.2 65.4 1.0 CG B:ASP447 3.3 84.1 1.0 CE1 B:HIS119 3.3 68.8 1.0 CD2 B:HIS117 3.4 69.8 1.0 OD2 B:ASP447 3.5 101.4 1.0 CE1 B:HIS390 3.5 73.9 1.0 ND1 B:HIS117 4.3 72.7 1.0 ND1 B:HIS362 4.3 62.3 1.0 ND1 B:HIS390 4.4 71.7 1.0 CG B:HIS119 4.4 74.1 1.0 CG B:HIS362 4.4 72.5 1.0 ND1 B:HIS119 4.4 61.9 1.0 CG B:HIS117 4.5 59.3 1.0 NE2 B:HIS390 4.5 84.4 1.0 O B:HOH702 4.7 49.7 1.0 CB B:ASP447 4.7 62.0 1.0

G.Kaur, J.R.Horton, G.Tzertzinis, J.Zhou, I.Schildkraut, X.Cheng. Structural Basis For the Substrate Specificity of Helix Pomatia Amp Deaminase and A Chimeric Adgf Adenosine Deaminase. J.Biol.Chem. 10357 2025.
ISSN: ESSN 1083-351X
PubMed: 40505866
DOI: 10.1016/J.JBC.2025.110357