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Chlorine in PDB 9gkz: Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35

Protein crystallography data

The structure of Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35, PDB code: 9gkz 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) 73.67 / 2.72
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 147.342, 48.858, 82.249, 90, 90, 90
R / Rfree (%) 15.6 / 23.3

Other elements in 9gkz:

The structure of Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35 also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Potassium (K) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35 (pdb code 9gkz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35, PDB code: 9gkz:

Chlorine binding site 1 out of 1 in 9gkz

Go back to Chlorine Binding Sites List in 9gkz
Chlorine binding site 1 out of 1 in the Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Acetylpolyamine Amidohydrolase (Apah) From Pseudomonas Sp. M30-35 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:50.0
occ:1.00
ZN A:ZN405 2.7 30.6 1.0
NE2 A:HIS159 3.5 31.8 1.0
NE2 A:HIS158 3.7 33.7 1.0
O A:HOH560 3.7 31.3 1.0
CA A:GLY321 3.8 30.6 1.0
CD2 A:HIS159 3.9 32.0 1.0
OD1 A:ASP195 3.9 32.2 1.0
OD2 A:ASP195 4.2 31.5 1.0
N A:GLY321 4.2 31.7 1.0
ND1 A:HIS197 4.3 33.6 1.0
OD2 A:ASP284 4.3 32.0 1.0
CD2 A:HIS158 4.4 32.8 1.0
CG A:ASP195 4.4 29.6 1.0
O A:HOH553 4.4 39.1 1.0
CE1 A:HIS159 4.6 28.4 1.0
O A:GLY167 4.6 34.0 1.0
CG A:PRO156 4.7 33.3 1.0
CE1 A:HIS158 4.7 27.1 1.0
CG A:HIS197 4.9 28.6 1.0
CE1 A:HIS197 4.9 31.4 1.0
CB A:PRO156 5.0 31.6 1.0
CB A:HIS197 5.0 26.5 1.0

Reference:

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.
Page generated: Sun Jul 13 16:57:07 2025

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