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Arsenic in PDB 7r3f: Monomeric Pqse Mutant E187R

Enzymatic activity of Monomeric Pqse Mutant E187R

All present enzymatic activity of Monomeric Pqse Mutant E187R:
3.1.2.32;

Protein crystallography data

The structure of Monomeric Pqse Mutant E187R, PDB code: 7r3f was solved by S.R.Borgert, S.Schmelz, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.29 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.535, 60.174, 128.262, 90, 90, 90
R / Rfree (%) 20.4 / 23.9

Other elements in 7r3f:

The structure of Monomeric Pqse Mutant E187R also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Monomeric Pqse Mutant E187R (pdb code 7r3f). 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 Monomeric Pqse Mutant E187R, PDB code: 7r3f:

Arsenic binding site 1 out of 1 in 7r3f

Go back to Arsenic Binding Sites List in 7r3f
Arsenic binding site 1 out of 1 in the Monomeric Pqse Mutant E187R


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Monomeric Pqse Mutant E187R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As403

b:29.4
occ:1.00
AS A:CAC403 0.0 29.4 1.0
O2 A:CAC403 1.7 27.0 1.0
O1 A:CAC403 1.7 14.5 1.0
C1 A:CAC403 2.0 16.0 1.0
C2 A:CAC403 2.0 14.6 1.0
O A:HOH514 2.9 10.0 1.0
FE A:FE402 3.2 11.4 1.0
HE2 A:PHE212 3.6 14.5 1.0
FE A:FE401 3.6 10.3 1.0
HE1 A:HIS176 3.7 7.8 1.0
OD2 A:ASP195 3.8 8.5 1.0
O A:HOH668 3.8 23.3 1.0
HD13 A:LEU210 3.9 14.5 1.0
HD22 A:LEU294 4.0 17.4 1.0
OD2 A:ASP90 4.0 9.0 1.0
CE1 A:HIS176 4.4 6.5 1.0
HE1 A:PHE293 4.4 12.9 1.0
OD1 A:ASP90 4.5 9.3 1.0
CE2 A:PHE212 4.5 12.1 1.0
HD22 A:LEU210 4.6 10.7 1.0
O A:HOH723 4.6 26.7 1.0
CG A:ASP195 4.6 8.8 1.0
NE2 A:HIS238 4.6 7.6 1.0
NE2 A:HIS176 4.6 6.3 1.0
CG A:ASP90 4.7 7.4 1.0
ND1 A:HIS88 4.8 7.7 1.0
CD1 A:LEU210 4.8 12.1 1.0
HD11 A:LEU210 4.8 14.5 1.0
CD2 A:LEU294 4.9 14.5 1.0
HD13 A:LEU294 4.9 15.3 1.0

Reference:

S.R.Borgert, S.Henke, F.Witzgall, S.Schmelz, S.Zur Lage, S.K.Hotop, S.Stephen, D.Lubken, J.Kruger, N.O.Gomez, M.Van Ham, L.Jansch, M.Kalesse, A.Pich, M.Bronstrup, S.Haussler, W.Blankenfeldt. Moonlighting Chaperone Activity of the Enzyme Pqse Contributes to Rhlr-Controlled Virulence of Pseudomonas Aeruginosa. Nat Commun V. 13 7402 2022.
ISSN: ESSN 2041-1723
PubMed: 36456567
DOI: 10.1038/S41467-022-35030-W
Page generated: Wed Jul 10 13:51:20 2024

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