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Chlorine in PDB 5g1m: Crystal Structure of Nagz From Pseudomonas Aeruginosa

Enzymatic activity of Crystal Structure of Nagz From Pseudomonas Aeruginosa

All present enzymatic activity of Crystal Structure of Nagz From Pseudomonas Aeruginosa:
3.2.1.52;

Protein crystallography data

The structure of Crystal Structure of Nagz From Pseudomonas Aeruginosa, PDB code: 5g1m was solved by I.Acebron, C.Artola-Recolons, K.Mahasenan, S.Mobashery, J.A.Hermoso, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.96 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.971, 75.289, 76.389, 90.00, 110.10, 90.00
R / Rfree (%) 19.6 / 24.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Nagz From Pseudomonas Aeruginosa (pdb code 5g1m). 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 Nagz From Pseudomonas Aeruginosa, PDB code: 5g1m:

Chlorine binding site 1 out of 1 in 5g1m

Go back to Chlorine Binding Sites List in 5g1m
Chlorine binding site 1 out of 1 in the Crystal Structure of Nagz From Pseudomonas Aeruginosa


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 Nagz From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1333

b:58.5
occ:1.00
O A:ALA154 3.7 17.9 1.0
C A:ALA154 4.0 12.4 1.0
CA A:GLY155 4.2 11.3 1.0
N A:GLY155 4.2 14.9 1.0
O A:LYS305 4.3 19.8 1.0
N A:GLY306 4.3 18.7 1.0
O A:HOH2144 4.3 18.0 1.0
C A:LYS305 4.4 21.3 1.0
CA A:GLY306 4.4 19.4 1.0
O A:ALA153 4.6 17.2 1.0
CB A:LYS305 4.7 23.4 1.0
CA A:ALA154 4.8 12.2 1.0
O A:HOH2141 5.0 20.9 1.0

Reference:

I.Acebron, K.V.Mahasenan, S.De Benedetti, M.Lee, C.Artola-Recolons, D.Hesek, H.Wang, J.A.Hermoso, S.Mobashery. Catalytic Cycle of the N-Acetylglucosaminidase Nagz From Pseudomonas Aeruginosa. J. Am. Chem. Soc. V. 139 6795 2017.
ISSN: ESSN 1520-5126
PubMed: 28482153
DOI: 10.1021/JACS.7B01626
Page generated: Sat Jul 12 02:23:23 2025

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