Chlorine in PDB 6flm: Crystal Structure of the Human TRIM25 Pryspry Domain

All present enzymatic activity of Crystal Structure of the Human TRIM25 Pryspry Domain:
2.3.2.27;

The structure of Crystal Structure of the Human TRIM25 Pryspry Domain, PDB code: 6flm was solved by S.Cusack, E.Kowalinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.74 / 2.01
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	152.750, 152.750, 68.960, 90.00, 90.00, 120.00
R / Rfree (%)	16.5 / 20.6

The binding sites of Chlorine atom in the Crystal Structure of the Human TRIM25 Pryspry Domain (pdb code 6flm). 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 the Human TRIM25 Pryspry Domain, PDB code: 6flm:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Human TRIM25 Pryspry Domain


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 the Human TRIM25 Pryspry Domain within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl706 b:16.9 occ:1.00 O C:HOH887 3.2 21.3 1.0 O C:HOH948 3.2 30.3 1.0 NE1 C:TRP616 3.2 13.2 1.0 NH1 C:ARG541 3.3 19.5 1.0 N C:SER499 3.4 15.6 1.0 OG C:SER499 3.5 22.6 1.0 CA C:CYS498 3.7 16.5 1.0 CD1 C:PHE618 3.9 18.7 1.0 CB C:CYS498 4.0 13.2 1.0 C C:CYS498 4.1 14.3 1.0 CE2 C:TRP616 4.1 12.5 1.0 NH2 C:ARG541 4.1 15.7 1.0 CD1 C:TRP616 4.1 14.8 1.0 CZ C:ARG541 4.2 14.1 1.0 CE1 C:PHE618 4.3 16.3 1.0 CB C:SER499 4.3 15.1 1.0 CZ2 C:TRP616 4.4 15.0 1.0 O C:TYR497 4.4 15.9 1.0 CA C:SER499 4.5 15.3 1.0 SG C:CYS498 4.7 16.5 1.0 CG C:PHE618 4.7 16.7 1.0 N C:CYS498 4.9 14.0 1.0 CB C:PHE618 5.0 19.0 1.0

M.G.Koliopoulos, M.Lethier, A.G.Van Der Veen, K.Haubrich, J.Hennig, E.Kowalinski, R.V.Stevens, S.R.Martin, C.Reis E Sousa, S.Cusack, K.Rittinger. Molecular Mechanism of Influenza A NS1-Mediated TRIM25 Recognition and Inhibition. Nat Commun V. 9 1820 2018.
ISSN: ESSN 2041-1723
PubMed: 29739942
DOI: 10.1038/S41467-018-04214-8