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Chlorine in PDB 4hxf: Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone

Enzymatic activity of Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone

All present enzymatic activity of Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone:
3.4.19.1;

Protein crystallography data

The structure of Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone, PDB code: 4hxf was solved by A.Kiss-Szeman, D.K.Menyhard, E.Tichy-Racs, B.Hornung, K.Radi, Z.Szeltner, K.Domokos, I.Szamosi, G.Naray-Szabo, L.Polgar, V.Harmat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.74 / 1.60
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 184.057, 184.057, 145.529, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 18.6

Other elements in 4hxf:

The structure of Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone (pdb code 4hxf). 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 Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone, PDB code: 4hxf:

Chlorine binding site 1 out of 1 in 4hxf

Go back to Chlorine Binding Sites List in 4hxf
Chlorine binding site 1 out of 1 in the Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Acylaminoacyl Peptidase in Complex with Z-Gly-Gly-Phe-Chloromethyl Ketone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl717

b:19.5
occ:1.00
 O B:HOH1182 3.1 17.4 0.5
O B:HOH933 3.2 27.9 1.0
O B:HOH1182 3.6 26.3 0.5
CG B:GLU160 3.7 16.7 1.0
NZ B:LYS98 3.8 14.9 1.0
CA B:GLU160 3.9 13.7 1.0
CE B:LYS98 4.0 16.1 1.0
O B:THR159 4.2 15.6 1.0
CB B:GLU160 4.3 15.4 1.0
N B:GLU160 4.5 14.2 1.0
C B:THR159 4.6 14.7 1.0
CD B:GLU160 4.6 18.9 1.0
NZ B:LYS72 4.8 23.7 1.0
O B:GLU160 4.9 14.9 1.0
C B:GLU160 5.0 15.6 1.0
O B:HOH946 5.0 24.9 1.0

Reference:

D.K.Menyhard, A.Kiss-Szeman, E.Tichy-Racs, B.Hornung, K.Radi, Z.Szeltner, K.Domokos, I.Szamosi, G.Naray-Szabo, L.Polgar, V.Harmat. A Self-Compartmentalizing Hexamer Serine Protease From Pyrococcus Horikoshii: Substrate Selection Achieved Through Multimerization. J.Biol.Chem. V. 288 17884 2013.
ISSN: ISSN 0021-9258
PubMed: 23632025
DOI: 10.1074/JBC.M113.451534
Page generated: Fri Jul 11 16:35:06 2025

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