Zinc in PDB 9gl1: Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii

The structure of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii, PDB code: 9gl1 was solved by L.G.Graf, S.Schulze, G.J.Palm, M.Lammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.20 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	113.564, 113.564, 90.426, 90, 90, 120
R / Rfree (%)	23.7 / 26.6

The structure of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii (pdb code 9gl1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii, PDB code: 9gl1:

Zinc binding site 1 out of 1 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii


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 Acetylpolyamine Aminohydrolase (Apah) From Legionella Cherrii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:110.3 occ:1.00 OD1 A:ASP216 1.9 107.0 1.0 OD2 A:ASP329 2.0 107.5 1.0 OD1 A:ASN218 2.0 108.0 1.0 O A:HOH603 2.4 107.2 1.0 CG A:ASP216 2.5 109.0 1.0 OD2 A:ASP216 2.5 110.5 1.0 O A:HOH601 2.8 110.3 1.0 CG A:ASP329 3.0 108.5 1.0 CG A:ASN218 3.0 106.8 1.0 OD1 A:ASP329 3.4 107.8 1.0 CB A:ASN218 3.5 103.7 1.0 N A:ASN218 3.9 105.5 1.0 CB A:ASP216 4.0 107.5 1.0 CA A:GLY389 4.1 106.9 1.0 ND2 A:ASN218 4.2 108.5 1.0 NE2 A:HIS178 4.2 110.5 1.0 CG1 A:VAL217 4.3 107.8 1.0 N A:GLY389 4.3 111.7 1.0 CB A:ASP329 4.3 107.8 1.0 CA A:ASN218 4.3 102.3 1.0 CE1 A:HIS178 4.4 110.2 1.0 N A:VAL217 4.5 110.3 1.0 OH A:TYR391 4.7 106.7 1.0 CA A:ASP216 4.7 110.1 1.0 NE2 A:HIS179 4.7 109.4 1.0 C A:ASP216 4.8 106.4 1.0 SG A:CYS338 4.8 112.3 1.0 CE2 A:TYR391 4.9 106.8 1.0

L.G.Graf, C.Moreno-Yruela, C.Qin, S.Schulze, G.J.Palm, O.Schmoeker, N.Wang, D.Hocking, L.Jebeli, B.Girbardt, L.Berndt, D.M.Weis, M.Janetzky, D.Zuehlke, S.Sievers, R.A.Strugnell, C.A.Olsen, K.Hofmann, M.Lammers. Distribution and Diversity of Classical Deacylases in Bacteria Nature Communications 2024.