Bromine in PDB 5u7b: Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin.

Enzymatic activity of Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin.

All present enzymatic activity of Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin.:
4.99.1.2;

Protein crystallography data

The structure of Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin., PDB code: 5u7b was solved by H.M.Wahba, M.Stevenson, A.Mansour, J.Sygusch, D.E.Wilcox, J.G.Omichinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.50 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.860, 88.802, 55.010, 90.00, 97.19, 90.00
R / Rfree (%) 16.5 / 22.4

Other elements in 5u7b:

The structure of Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin. also contains other interesting chemical elements:

Tin (Sn) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin. (pdb code 5u7b). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin., PDB code: 5u7b:

Bromine binding site 1 out of 1 in 5u7b

Go back to Bromine Binding Sites List in 5u7b
Bromine binding site 1 out of 1 in the Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of A the Tin-Bound Form of Merb Formed From Diethyltin. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br301

b:53.8
occ:0.61
 HB3 A:LYS2 2.7 66.2 1.0
HD3 A:PRO5 2.9 38.5 1.0
HB3 A:ALA4 3.4 44.8 1.0
CB A:LYS2 3.5 55.2 1.0
HG3 A:PRO5 3.5 43.1 1.0
HD3 A:LYS2 3.7 71.5 1.0
CD A:PRO5 3.7 32.0 1.0
HB2 A:LYS2 3.7 66.2 1.0
HG3 A:LYS2 3.8 69.1 1.0
HG2 A:PRO5 3.9 43.1 1.0
CG A:PRO5 3.9 35.9 1.0
HD2 A:LYS2 4.0 71.5 1.0
CG A:LYS2 4.0 57.6 1.0
HD2 A:PRO5 4.0 38.5 1.0
CD A:LYS2 4.1 59.6 1.0
CB A:ALA4 4.4 37.3 1.0
H A:ALA4 4.5 41.4 1.0
HB2 A:ALA4 4.6 44.8 1.0
CA A:LYS2 4.7 54.4 1.0
HA A:LYS2 4.8 65.3 1.0
HB1 A:ALA4 4.8 44.8 1.0
N A:PRO5 4.9 33.7 1.0
C A:LYS2 4.9 44.8 1.0
HG2 A:LYS2 4.9 69.1 1.0
O A:HOH417 5.0 37.4 1.0

Reference:

H.M.Wahba, M.J.Stevenson, A.Mansour, J.Sygusch, D.E.Wilcox, J.G.Omichinski. Structural and Biochemical Characterization of Organotin and Organolead Compounds Binding to the Organomercurial Lyase Merb Provide New Insights Into Its Mechanism of Carbon-Metal Bond Cleavage. J. Am. Chem. Soc. V. 139 910 2017.
ISSN: ESSN 1520-5126
PubMed: 27989130
DOI: 10.1021/JACS.6B11327
Page generated: Sat Dec 12 02:31:05 2020

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