Atomistry » Arsenic » PDB 4uhf-4zng » 4xay
Atomistry »
  Arsenic »
    PDB 4uhf-4zng »
      4xay »

Arsenic in PDB 4xay: Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes

Protein crystallography data

The structure of Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes, PDB code: 4xay was solved by C.J.Jackson, E.Campbell, M.Kaltenbach, N.Tokuriki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.41 / 1.84
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 85.763, 85.923, 88.680, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 21.9

Other elements in 4xay:

The structure of Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes (pdb code 4xay). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes, PDB code: 4xay:

Arsenic binding site 1 out of 1 in 4xay

Go back to Arsenic Binding Sites List in 4xay
Arsenic binding site 1 out of 1 in the Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Cycles of Destabilization and Repair Underlie Evolutionary Transitions in Enzymes within 5.0Å range:
probe atom residue distance (Å) B Occ
G:As401

b:32.9
occ:0.60
AS G:CAC401 0.0 32.9 0.6
O2 G:CAC401 1.7 12.3 0.6
O1 G:CAC401 1.7 33.9 0.6
C2 G:CAC401 2.0 32.0 0.6
C1 G:CAC401 2.0 21.2 0.6
ZN G:ZN403 3.0 25.3 1.0
ZN G:ZN402 3.3 19.1 1.0
OD2 G:ASP301 3.7 24.4 1.0
OQ2 G:KCX169 3.8 27.6 1.0
CE1 G:HIS201 4.0 30.2 1.0
ND1 G:HIS201 4.0 22.6 1.0
OQ1 G:KCX169 4.1 19.9 1.0
OD1 G:ASP301 4.2 19.9 1.0
NE1 G:TRP131 4.3 19.6 1.0
NE2 G:HIS230 4.3 19.3 1.0
CX G:KCX169 4.4 27.2 1.0
CG G:ASP301 4.4 25.8 1.0
NE2 G:HIS57 4.4 17.1 1.0
NH1 G:ARG254 4.7 30.5 1.0
CE2 G:TRP131 4.9 22.7 1.0
CZ2 G:TRP131 4.9 22.8 1.0
CE1 G:HIS230 4.9 25.2 1.0

Reference:

E.Campbell, M.Kaltenbach, G.J.Correy, P.D.Carr, B.T.Porebski, E.K.Livingstone, L.Afriat-Jurnou, A.M.Buckle, M.Weik, F.Hollfelder, N.Tokuriki, C.J.Jackson. The Role of Protein Dynamics in the Evolution of New Enzyme Function. Nat.Chem.Biol. V. 12 944 2016.
ISSN: ESSN 1552-4469
PubMed: 27618189
DOI: 10.1038/NCHEMBIO.2175
Page generated: Sat Dec 12 01:45:50 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