Chlorine in PDB 3tv1: Crystal Structure of Rtca.Amp Product Complex

All present enzymatic activity of Crystal Structure of Rtca.Amp Product Complex:
6.5.1.4;

The structure of Crystal Structure of Rtca.Amp Product Complex, PDB code: 3tv1 was solved by A.K.Chakravarty, P.Smith, S.Shuman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.91 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.160, 79.810, 85.670, 90.00, 103.65, 90.00
R / Rfree (%)	18 / 23.3

The binding sites of Chlorine atom in the Crystal Structure of Rtca.Amp Product Complex (pdb code 3tv1). 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 Rtca.Amp Product Complex, PDB code: 3tv1:

Chlorine binding site 1 out of 1 in the Crystal Structure of Rtca.Amp Product Complex


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 Rtca.Amp Product Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl851 b:22.5 occ:1.00 O2 B:PEG991 2.2 31.3 1.0 O B:HOH728 2.9 26.8 1.0 N B:ALA133 3.2 16.4 1.0 N B:ASP126 3.3 13.0 1.0 CB B:THR125 3.5 13.0 1.0 C3 B:PEG991 3.5 20.5 1.0 CA B:THR125 3.7 15.5 1.0 CA B:PRO132 3.8 15.5 1.0 O B:HOH482 3.8 19.6 1.0 CB B:ALA133 3.9 14.2 1.0 C B:PRO132 4.0 18.4 1.0 C B:THR125 4.0 16.2 1.0 CD1 B:LEU155 4.1 15.9 1.0 CG2 B:THR100 4.1 11.2 1.0 CA B:ALA133 4.1 18.7 1.0 C4 B:PEG991 4.1 22.3 1.0 CG2 B:THR125 4.1 15.6 1.0 O B:HOH707 4.3 17.1 1.0 CA B:ASP126 4.3 16.7 1.0 O B:PRO131 4.4 15.2 1.0 O4 B:PEG991 4.5 32.9 1.0 OG1 B:THR125 4.6 12.8 1.0 CB B:PRO132 4.7 21.8 1.0 CG2 B:VAL168 4.7 12.6 1.0 OD2 B:ASP126 4.9 18.8 1.0 N B:PRO132 4.9 15.8 1.0 CG B:ASP126 4.9 14.3 1.0 OG1 B:THR100 4.9 12.5 1.0

A.K.Chakravarty, P.Smith, S.Shuman. Structures of Rna 3'-Phosphate Cyclase Bound to Atp Reveal the Mechanism of Nucleotidyl Transfer and Metal-Assisted Catalysis. Proc.Natl.Acad.Sci.Usa V. 108 21034 2011.
ISSN: ISSN 0027-8424
PubMed: 22167800
DOI: 10.1073/PNAS.1115560108