Chlorine in PDB 5uvf: Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870

Enzymatic activity of Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870

All present enzymatic activity of Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870, PDB code: 5uvf was solved by R.M.Counago, C.Bountra, P.Arruda, A.M.Edwards, O.Gileadi, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.66 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 92.141, 95.242, 192.040, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.4

Other elements in 5uvf:

The structure of Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870 also contains other interesting chemical elements:

Fluorine (F) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870 (pdb code 5uvf). 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 Vaccinia-Related Kinase Bound to Bi- D1870, PDB code: 5uvf:

Chlorine binding site 1 out of 1 in 5uvf

Go back to Chlorine Binding Sites List in 5uvf
Chlorine binding site 1 out of 1 in the Crystal Structure of the Human Vaccinia-Related Kinase Bound to Bi- D1870


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 Vaccinia-Related Kinase Bound to Bi- D1870 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl407

b:85.0
occ:1.00
NE2 C:HIS258 3.6 57.8 1.0
NH2 C:ARG148 3.7 54.6 1.0
NH1 C:ARG148 3.8 50.7 1.0
CE1 C:HIS258 4.1 57.3 1.0
CZ C:ARG148 4.2 66.4 1.0
CD2 C:HIS258 4.7 56.6 1.0

Reference:

R.M.Counago, C.K.Allerston, P.Savitsky, H.Azevedo, P.H.Godoi, C.I.Wells, A.Mascarello, F.H.De Souza Gama, K.B.Massirer, W.J.Zuercher, C.R.W.Guimaraes, O.Gileadi. Structural Characterization of Human Vaccinia-Related Kinases (Vrk) Bound to Small-Molecule Inhibitors Identifies Different P-Loop Conformations. Sci Rep V. 7 7501 2017.
ISSN: ESSN 2045-2322
PubMed: 28790404
DOI: 10.1038/S41598-017-07755-Y
Page generated: Sat Dec 12 12:32:31 2020

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