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Chlorine in PDB 4re5: Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor

Enzymatic activity of Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor

All present enzymatic activity of Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor:
3.4.19.1;

Protein crystallography data

The structure of Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor, PDB code: 4re5 was solved by D.K.Menyhard, Z.Orgovan, Z.Szeltner, I.Szamosi, V.Harmat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.93 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.813, 104.430, 170.080, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor (pdb code 4re5). 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 Complexed with A Chloromethylketone Inhibitor, PDB code: 4re5:

Chlorine binding site 1 out of 1 in 4re5

Go back to Chlorine Binding Sites List in 4re5
Chlorine binding site 1 out of 1 in the Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Acylaminoacyl Peptidase Complexed with A Chloromethylketone Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl604

b:75.0
occ:1.00
CG1 A:VAL39 4.4 25.2 1.0
N A:PHE41 4.5 24.9 1.0
O A:LYS24 4.6 25.1 1.0
O A:VAL39 4.7 24.2 1.0
CB A:PHE41 4.7 28.4 1.0
CB A:SER26 4.8 27.0 1.0
CG2 A:VAL46 4.9 25.9 1.0
CG1 A:VAL46 4.9 25.1 1.0

Reference:

D.K.Menyhard, Z.Orgovan, Z.Szeltner, I.Szamosi, V.Harmat. Catalytically Distinct States Captured in A Crystal Lattice: the Substrate-Bound and Scavenger States of Acylaminoacyl Peptidase and Their Implications For Functionality Acta Crystallogr.,Sect.D V. 71 2015.
ISSN: ESSN 1399-0047
DOI: 10.1107/S1399004714026819
Page generated: Fri Jul 11 21:19:44 2025

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