Atomistry » Bromine » PDB 5cc3-5ev2 » 5dsf
Atomistry »
  Bromine »
    PDB 5cc3-5ev2 »
      5dsf »

Bromine in PDB 5dsf: Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S

Enzymatic activity of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S

All present enzymatic activity of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S:
4.99.1.2;

Protein crystallography data

The structure of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S, PDB code: 5dsf was solved by H.M.Wahba, L.Lecoq, M.Stevenson, A.Mansour, L.Cappadocia, J.Lafrance-Vanasse, K.J.Wilkinson, 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) 37.00 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.680, 88.349, 52.671, 90.00, 100.93, 90.00
R / Rfree (%) 16.5 / 20.8

Other elements in 5dsf:

The structure of Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S (pdb code 5dsf). 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 the Mercury-Bound Form of Merb Mutant D99S, PDB code: 5dsf:

Bromine binding site 1 out of 1 in 5dsf

Go back to Bromine Binding Sites List in 5dsf
Bromine binding site 1 out of 1 in the Crystal Structure of the Mercury-Bound Form of Merb Mutant D99S


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 the Mercury-Bound Form of Merb Mutant D99S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br302

b:44.6
occ:0.66
HE3 A:LYS2 2.9 64.5 1.0
HD3 A:PRO5 2.9 37.6 1.0
HB3 A:LYS2 3.1 47.4 1.0
HE2 A:LYS2 3.3 64.5 1.0
HD3 A:LYS2 3.3 61.0 1.0
HB3 A:ALA4 3.3 36.3 1.0
CE A:LYS2 3.4 53.8 1.0
HG3 A:PRO5 3.7 37.0 1.0
CD A:PRO5 3.7 31.3 1.0
CD A:LYS2 3.8 50.8 1.0
HD2 A:PRO5 3.9 37.6 1.0
CB A:LYS2 4.0 39.5 1.0
HB2 A:LYS2 4.1 47.4 1.0
CG A:PRO5 4.2 30.8 1.0
CB A:ALA4 4.3 30.3 1.0
CG A:LYS2 4.5 37.7 1.0
HB2 A:ALA4 4.5 36.3 1.0
H A:ALA4 4.5 35.8 1.0
HD2 A:LYS2 4.7 61.0 1.0
HG2 A:PRO5 4.7 37.0 1.0
HB1 A:ALA4 4.7 36.3 1.0
HG2 A:LYS2 4.7 45.2 1.0
NZ A:LYS2 4.8 52.2 1.0
O A:HOH428 4.9 42.8 1.0
N A:PRO5 4.9 31.0 1.0
HZ1 A:LYS2 4.9 62.6 1.0

Reference:

H.M.Wahba, L.Lecoq, M.Stevenson, A.Mansour, L.Cappadocia, J.Lafrance-Vanasse, K.J.Wilkinson, J.Sygusch, D.E.Wilcox, J.G.Omichinski. Structural and Biochemical Characterization of A Copper-Binding Mutant of the Organomercurial Lyase Merb: Insight Into the Key Role of the Active Site Aspartic Acid in Hg-Carbon Bond Cleavage and Metal Binding Specificity. Biochemistry V. 55 1070 2016.
ISSN: ISSN 0006-2960
PubMed: 26820485
DOI: 10.1021/ACS.BIOCHEM.5B01298
Page generated: Wed Jul 10 23:27:17 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy