Chlorine in PDB 6d31: Structure of Human USB1 with Adenosine 5'-Monophosphate

Protein crystallography data

The structure of Structure of Human USB1 with Adenosine 5'-Monophosphate, PDB code: 6d31 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) 44.39 / 1.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.430, 52.077, 46.240, 90.00, 106.26, 90.00
R / Rfree (%) 14.7 / 18.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Human USB1 with Adenosine 5'-Monophosphate (pdb code 6d31). 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 Adenosine 5'-Monophosphate, PDB code: 6d31:

Chlorine binding site 1 out of 1 in 6d31

Go back to Chlorine Binding Sites List in 6d31
Chlorine binding site 1 out of 1 in the Structure of Human USB1 with Adenosine 5'-Monophosphate


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 Adenosine 5'-Monophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:15.7
occ:1.00
HH21 A:ARG112 2.5 20.5 1.0
H A:ARG112 2.6 17.2 1.0
HG2 A:ARG112 2.7 16.8 1.0
HD2 A:PRO111 2.8 19.7 1.0
HB3 A:ARG112 3.1 17.6 1.0
O A:HOH585 3.1 28.9 1.0
NH2 A:ARG112 3.2 17.1 1.0
HD3 A:ARG112 3.3 19.1 1.0
HG13 A:VAL110 3.4 20.0 1.0
N A:ARG112 3.4 14.4 1.0
CG A:ARG112 3.4 14.0 1.0
HB2 A:PRO111 3.5 20.6 1.0
HH22 A:ARG112 3.5 20.5 1.0
CD A:PRO111 3.5 16.4 1.0
N A:PRO111 3.7 15.9 1.0
CB A:ARG112 3.7 14.7 1.0
HA A:VAL110 3.7 18.9 1.0
CD A:ARG112 3.8 16.0 1.0
HG12 A:VAL110 3.9 20.0 1.0
CG1 A:VAL110 4.1 16.6 1.0
CB A:PRO111 4.1 17.2 1.0
CA A:ARG112 4.1 15.0 1.0
C A:VAL110 4.2 15.7 1.0
HG2 A:PRO111 4.2 21.3 1.0
CA A:PRO111 4.2 15.6 1.0
CG A:PRO111 4.3 17.8 1.0
C A:PRO111 4.3 14.9 1.0
HG3 A:ARG112 4.3 16.8 1.0
CZ A:ARG112 4.3 16.1 1.0
HD3 A:PRO111 4.3 19.7 1.0
CA A:VAL110 4.3 15.7 1.0
NE A:ARG112 4.5 16.0 1.0
HB2 A:ARG112 4.5 17.6 1.0
O A:HOH510 4.6 26.7 1.0
HA A:ARG112 4.7 17.9 1.0
HD2 A:ARG112 4.7 19.1 1.0
HG11 A:VAL110 4.8 20.0 1.0
CB A:VAL110 4.8 15.9 1.0
O A:VAL110 4.9 14.9 1.0

Reference:

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
Page generated: Sat Dec 12 12:52:08 2020

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