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Chlorine in PDB 5xev: Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans

Enzymatic activity of Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans

All present enzymatic activity of Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans:
3.4.13.9;

Protein crystallography data

The structure of Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans, PDB code: 5xev was solved by V.N.Are, A.Kumar, B.Ghosh, R.D.Makde, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.96 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.670, 91.879, 53.849, 90.00, 98.78, 90.00
R / Rfree (%) 14.6 / 16.4

Other elements in 5xev:

The structure of Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans (pdb code 5xev). 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 A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans, PDB code: 5xev:

Chlorine binding site 1 out of 1 in 5xev

Go back to Chlorine Binding Sites List in 5xev
Chlorine binding site 1 out of 1 in the Crystal Structure of A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans


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 A Novel Xaa-Pro Dipeptidase From Deinococcus Radiodurans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:18.6
occ:1.00
 HE A:ARG46 2.3 42.9 1.0
H A:ARG47 2.3 15.6 1.0
HA A:ARG46 2.9 20.4 1.0
HD2 A:ARG47 3.0 17.4 1.0
O A:HOH960 3.1 26.9 1.0
HE1 A:PHE25 3.1 15.3 1.0
O A:HOH854 3.1 22.4 1.0
NE A:ARG46 3.2 35.7 1.0
N A:ARG47 3.2 13.0 1.0
HB3 A:ARG47 3.3 14.0 1.0
HH21 A:ARG46 3.3 47.1 1.0
HB3 A:ARG46 3.4 18.1 1.0
HG2 A:ARG47 3.5 15.0 1.0
HD1 A:PHE25 3.5 15.1 1.0
CA A:ARG46 3.7 17.0 1.0
CE1 A:PHE25 3.8 12.8 1.0
HD2 A:ARG46 3.8 32.7 1.0
CD A:ARG47 3.8 14.5 1.0
CB A:ARG47 3.8 11.7 1.0
CG A:ARG47 3.9 12.5 1.0
NH2 A:ARG46 3.9 39.2 1.0
C A:ARG46 4.0 14.8 1.0
CB A:ARG46 4.0 15.1 1.0
CD1 A:PHE25 4.0 12.6 1.0
CZ A:ARG46 4.0 40.1 1.0
CD A:ARG46 4.0 27.3 1.0
CA A:ARG47 4.1 12.7 1.0
HD3 A:ARG47 4.3 17.4 1.0
O A:THR45 4.6 19.6 1.0
CG A:ARG46 4.6 17.6 1.0
HH22 A:ARG46 4.7 47.1 1.0
HA A:ARG47 4.7 15.2 1.0
HB2 A:ARG47 4.7 14.0 1.0
HB2 A:ARG46 4.8 18.1 1.0
HG3 A:ARG47 4.8 15.0 1.0
NE A:ARG47 4.8 17.3 1.0
HD3 A:ARG46 4.8 32.7 1.0
O A:HOH832 4.9 26.8 1.0
HD22 A:ASN63 4.9 26.3 1.0
N A:ARG46 4.9 16.0 1.0
CZ A:PHE25 4.9 13.7 1.0
HG3 A:ARG46 5.0 21.1 1.0

Reference:

V.N.Are, S.N.Jamdar, B.Ghosh, V.D.Goyal, A.Kumar, S.Neema, R.Gadre, R.D.Makde. Crystal Structure of A Novel Prolidase From Deinococcus Radiodurans Identifies New Subfamily of Bacterial Prolidases. Proteins V. 85 2239 2017.
ISSN: ESSN 1097-0134
PubMed: 28929533
DOI: 10.1002/PROT.25389
Page generated: Fri Jul 26 20:54:18 2024

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