Chlorine in PDB 6d2z: Structure of Human USB1 with Uridine-Adenosine, Inactive H208Q Mutant

The structure of Structure of Human USB1 with Uridine-Adenosine, Inactive H208Q Mutant, PDB code: 6d2z was solved by Y.Nomura, E.J.Montemayor, S.E.Butcher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.53 / 1.18
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.393, 51.045, 46.299, 90.00, 105.88, 90.00
R / Rfree (%)	14.5 / 17.4

The binding sites of Chlorine atom in the Structure of Human USB1 with Uridine-Adenosine, Inactive H208Q Mutant (pdb code 6d2z). 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 Structure of Human USB1 with Uridine-Adenosine, Inactive H208Q Mutant, PDB code: 6d2z:

Chlorine binding site 1 out of 1 in the Structure of Human USB1 with Uridine-Adenosine, Inactive H208Q Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human USB1 with Uridine-Adenosine, Inactive H208Q Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:14.8 occ:1.00 HH21 A:ARG112 2.4 20.1 1.0 H A:ARG112 2.6 17.1 1.0 HD2 A:PRO111 2.7 19.1 1.0 HG2 A:ARG112 2.8 17.3 1.0 HB3 A:ARG112 3.0 17.5 1.0 HD3 A:ARG112 3.2 18.2 1.0 NH2 A:ARG112 3.2 16.7 1.0 N A:ARG112 3.4 14.2 1.0 CG A:ARG112 3.4 14.4 1.0 HB2 A:PRO111 3.5 20.8 1.0 HH22 A:ARG112 3.5 20.1 1.0 HG13 A:VAL110 3.5 18.3 1.0 CD A:PRO111 3.5 15.9 1.0 CB A:ARG112 3.6 14.6 1.0 N A:PRO111 3.7 15.0 1.0 CD A:ARG112 3.8 15.2 1.0 HA A:VAL110 3.9 17.9 1.0 HG12 A:VAL110 4.0 18.3 1.0 CA A:ARG112 4.1 14.1 1.0 CB A:PRO111 4.1 17.4 1.0 HG2 A:PRO111 4.2 20.8 1.0 CG1 A:VAL110 4.2 15.2 1.0 CG A:PRO111 4.2 17.4 1.0 C A:VAL110 4.2 14.3 1.0 C A:PRO111 4.2 14.9 1.0 CA A:PRO111 4.2 14.7 1.0 CZ A:ARG112 4.3 15.7 1.0 HD3 A:PRO111 4.3 19.1 1.0 HG3 A:ARG112 4.3 17.3 1.0 HB2 A:ARG112 4.5 17.5 1.0 NE A:ARG112 4.5 16.0 1.0 CA A:VAL110 4.5 14.9 1.0 HD2 A:ARG112 4.6 18.2 1.0 HA A:ARG112 4.6 16.9 1.0 O A:HOH459 4.7 36.2 1.0 O A:HOH498 4.9 36.6 1.0 HG11 A:VAL110 4.9 18.3 1.0 O A:VAL110 5.0 14.7 1.0 CB A:VAL110 5.0 15.5 1.0

Y.Nomura, D.Roston, E.J.Montemayor, Q.Cui, S.E.Butcher. Structural and Mechanistic Basis For Preferential Deadenylation of U6 Snrna By USB1. Nucleic Acids Res. V. 46 11488 2018.
ISSN: ESSN 1362-4962
PubMed: 30215753
DOI: 10.1093/NAR/GKY812