Atomistry » Bromine » PDB 5sv6-5u8a » 5u83
Atomistry »
  Bromine »
    PDB 5sv6-5u8a »
      5u83 »

Bromine in PDB 5u83: Crystal Structure of A Merb-Trimethytin Complex.

Enzymatic activity of Crystal Structure of A Merb-Trimethytin Complex.

All present enzymatic activity of Crystal Structure of A Merb-Trimethytin Complex.:
4.99.1.2;

Protein crystallography data

The structure of Crystal Structure of A Merb-Trimethytin Complex., PDB code: 5u83 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) 33.59 / 1.61
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.540, 89.072, 54.526, 90.00, 98.65, 90.00
R / Rfree (%) 15.9 / 20.1

Other elements in 5u83:

The structure of Crystal Structure of A Merb-Trimethytin Complex. 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 Merb-Trimethytin Complex. (pdb code 5u83). 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 Merb-Trimethytin Complex., PDB code: 5u83:

Bromine binding site 1 out of 1 in 5u83

Go back to Bromine Binding Sites List in 5u83
Bromine binding site 1 out of 1 in the Crystal Structure of A Merb-Trimethytin Complex.


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 Merb-Trimethytin Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br301

b:38.3
occ:0.49
HB3 B:LYS2 2.8 56.6 1.0
HD3 B:PRO5 2.9 24.1 1.0
HB3 B:ALA4 3.2 21.9 1.0
HD3 B:LYS2 3.3 66.3 1.0
O B:HOH557 3.4 38.4 1.0
CB B:LYS2 3.6 47.2 1.0
HB2 B:LYS2 3.6 56.6 1.0
CD B:PRO5 3.7 20.1 1.0
HG3 B:PRO5 3.7 24.9 1.0
CD B:LYS2 4.0 55.3 1.0
HD2 B:LYS2 4.0 66.3 1.0
CG B:PRO5 4.1 20.7 1.0
HD2 B:PRO5 4.1 24.1 1.0
CB B:ALA4 4.1 18.2 1.0
H B:ALA4 4.2 23.8 1.0
HG2 B:PRO5 4.2 24.9 1.0
HB2 B:ALA4 4.3 21.9 1.0
CG B:LYS2 4.3 51.1 1.0
HB1 B:ALA4 4.6 21.9 1.0
HG2 B:LYS2 4.6 61.3 1.0
CA B:LYS2 4.7 41.6 1.0
N B:ALA4 4.7 19.8 1.0
O B:LYS2 4.8 40.1 1.0
C B:LYS2 4.8 41.8 1.0
N B:PRO5 4.8 15.5 1.0
HA B:LYS2 4.9 49.9 1.0
CA B:ALA4 4.9 16.9 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 02:31:08 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy