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Arsenic in PDB 3htw: Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound

Protein crystallography data

The structure of Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound, PDB code: 3htw was solved by R.Hawwa, S.Larsen, K.Ratia, A.Mesecar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.292, 61.292, 206.011, 90.00, 90.00, 120.00
R / Rfree (%) 21.2 / 26

Other elements in 3htw:

The structure of Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound also contains other interesting chemical elements:

Cobalt (Co) 2 atoms
Magnesium (Mg) 7 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound (pdb code 3htw). 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 Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound, PDB code: 3htw:

Arsenic binding site 1 out of 1 in 3htw

Go back to Arsenic Binding Sites List in 3htw
Arsenic binding site 1 out of 1 in the Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Organophosphorus Hydrolase From Deinococcus Radiodurans with Cacodylate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1

b:48.2
occ:1.00
AS A:CAC1 0.0 48.2 1.0
O1 A:CAC1 1.6 51.5 1.0
O2 A:CAC1 1.7 48.4 1.0
C2 A:CAC1 1.9 48.5 1.0
C1 A:CAC1 1.9 49.0 1.0
CO A:CO2 3.3 30.8 1.0
CO A:CO424 3.4 30.8 1.0
OQ2 A:KCX243 3.4 29.2 1.0
OH A:TYR197 3.4 36.9 1.0
OQ1 A:KCX243 3.8 25.4 1.0
CZ A:TYR197 3.9 36.4 1.0
CE1 A:TYR197 4.0 34.2 1.0
CX A:KCX243 4.1 29.4 1.0
NH2 A:ARG328 4.2 42.7 1.0
NE2 A:HIS123 4.3 26.1 1.0
CE2 A:PHE126 4.4 30.9 1.0
OD2 A:ASP364 4.5 29.0 1.0
CZ A:PHE126 4.5 30.9 1.0
OD1 A:ASP364 4.6 30.4 1.0
ND1 A:HIS276 4.7 30.0 1.0
CE1 A:HIS123 4.9 27.1 1.0
CE2 A:TYR197 4.9 35.7 1.0
CD2 A:HIS123 5.0 25.1 1.0
CG A:ASP364 5.0 25.3 1.0

Reference:

R.Hawwa, S.D.Larsen, K.Ratia, A.D.Mesecar. Structure-Based and Random Mutagenesis Approaches Increase the Organophosphate-Degrading Activity of A Phosphotriesterase Homologue From Deinococcus Radiodurans. J.Mol.Biol. V. 393 36 2009.
ISSN: ISSN 0022-2836
PubMed: 19631223
DOI: 10.1016/J.JMB.2009.06.083
Page generated: Tue Oct 27 16:50:22 2020

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